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Conserved domains on  [gi|392896888|ref|NP_001255157|]
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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
224-351 3.59e-11

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 68.24  E-value: 3.59e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  224 EERKQFAILAKIQAEEKQRRLDEAKEKLAIDKEKL---RLKKEALQRELEERNKAERQKKMDDEERHREKERQKKAERDA 300
Cdd:PTZ00121 1339 EEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKeeaKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKK 1418
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 392896888  301 RLQFAKENA-AKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAER 351
Cdd:PTZ00121 1419 KADEAKKKAeEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAK 1470
 
Name Accession Description Interval E-value
PTZ00121 PTZ00121
MAEBL; Provisional
224-351 3.59e-11

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 68.24  E-value: 3.59e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  224 EERKQFAILAKIQAEEKQRRLDEAKEKLAIDKEKL---RLKKEALQRELEERNKAERQKKMDDEERHREKERQKKAERDA 300
Cdd:PTZ00121 1339 EEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKeeaKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKK 1418
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 392896888  301 RLQFAKENA-AKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAER 351
Cdd:PTZ00121 1419 KADEAKKKAeEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAK 1470
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
223-338 1.30e-10

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: 61.21  E-value: 1.30e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   223 EEERKQfailAKIQA--EEKQRRLDEAKEKLAIDKEKLRLKKEALQRELEERNKAERQKKMDDE-----ERHREKERQKK 295
Cdd:pfam05672   17 AEKRRQ----AREQRerEEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEErqrkaEEEAEEREQRE 92
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 392896888   296 AERDARLQFAKENAAKLAAQEAKkdislKSRLEQASMQQRERQ 338
Cdd:pfam05672   93 QEEQERLQKQKEEAEAKAREEAE-----RQRQEREKIMQQEEQ 130
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
174-357 3.13e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 64.96  E-value: 3.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  174 RQAQVRELFEHLANQTADKGKELRKFLSSILKEIHppedycikvyDPIGEEERKQFAILAKIQAEEKQRRLDEAKEKLAI 253
Cdd:COG1196   268 ELEELRLELEELELELEEAQAEEYELLAELARLEQ----------DIARLEERRRELEERLEELEEELAELEEELEELEE 337
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  254 DKEKLRLKKEALQRELEERNKAERQKK---MDDEERHREKERQKKAERDARLQFAKEnAAKLAAQEAKKDISLKSRLEQA 330
Cdd:COG1196   338 ELEELEEELEEAEEELEEAEAELAEAEealLEAEAELAEAEEELEELAEELLEALRA-AAELAAQLEELEEAEEALLERL 416
                         170       180
                  ....*....|....*....|....*..
gi 392896888  331 SMQQRERQKIDVQQAKLEAERILLLSK 357
Cdd:COG1196   417 ERLEEELEELEEALAELEEEEEEEEEA 443
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
223-351 7.25e-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: 59.09  E-value: 7.25e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   223 EEERKQFAILAKIQAEEKQRRLDEAKEKLAidKEKLRLKKEALQRELEERNK----AERQKKMDDEERHREKERQKKAER 298
Cdd:TIGR02794  108 EQAAKQAEEKQKQAEEAKAKQAAEAKAKAE--AEAERKAKEEAAKQAEEEAKakaaAEAKKKAEEAKKKAEAEAKAKAEA 185
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 392896888   299 DARlqfAKENAAKLAAQEAKKdislKSRLEQASMQQRERQKidvqQAKLEAER 351
Cdd:TIGR02794  186 EAK---AKAEEAKAKAEAAKA----KAAAEAAAKAEAEAAA----AAAAEAER 227
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
222-349 6.28e-05

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: 46.42  E-value: 6.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  222 GEEERKQFaiLAKIQAEEKQ-RRLDEAKEKLAIDKEKLRLKKEAL---QRELEERNKAERQKKMDDEERHREKERQ--KK 295
Cdd:cd16269   168 AEEVLQEF--LQSKEAEAEAiLQADQALTEKEKEIEAERAKAEAAeqeRKLLEEQQRELEQKLEDQERSYEEHLRQlkEK 245
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 392896888  296 AERDARLQfakenaaklaAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEA 349
Cdd:cd16269   246 MEEERENL----------LKEQERALESKLKEQEALLEEGFKEQAELLQEEIRS 289
 
Name Accession Description Interval E-value
PTZ00121 PTZ00121
MAEBL; Provisional
224-351 3.59e-11

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 68.24  E-value: 3.59e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  224 EERKQFAILAKIQAEEKQRRLDEAKEKLAIDKEKL---RLKKEALQRELEERNKAERQKKMDDEERHREKERQKKAERDA 300
Cdd:PTZ00121 1339 EEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKeeaKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKK 1418
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 392896888  301 RLQFAKENA-AKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAER 351
Cdd:PTZ00121 1419 KADEAKKKAeEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAK 1470
PTZ00121 PTZ00121
MAEBL; Provisional
170-351 4.00e-11

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 68.24  E-value: 4.00e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  170 IQKYRQAQVRELFEHLANQTAD---KGKELRKFLSSILKEihppedycikvydpigEEERKQFAILAKIQAEEKQR--RL 244
Cdd:PTZ00121 1589 AEEARIEEVMKLYEEEKKMKAEeakKAEEAKIKAEELKKA----------------EEEKKKVEQLKKKEAEEKKKaeEL 1652
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  245 DEAKEKLAIDKEKLRLKKEALQRELEERNKAERQKKMDDEERHREKERQKKAE----------RDARLQFAKENAAKLAA 314
Cdd:PTZ00121 1653 KKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEelkkkeaeekKKAEELKKAEEENKIKA 1732
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 392896888  315 QEAKKDISL-KSRLEQASMQQRERQKIdvQQAKLEAER 351
Cdd:PTZ00121 1733 EEAKKEAEEdKKKAEEAKKDEEEKKKI--AHLKKEEEK 1768
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
223-338 1.30e-10

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: 61.21  E-value: 1.30e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   223 EEERKQfailAKIQA--EEKQRRLDEAKEKLAIDKEKLRLKKEALQRELEERNKAERQKKMDDE-----ERHREKERQKK 295
Cdd:pfam05672   17 AEKRRQ----AREQRerEEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEErqrkaEEEAEEREQRE 92
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 392896888   296 AERDARLQFAKENAAKLAAQEAKkdislKSRLEQASMQQRERQ 338
Cdd:pfam05672   93 QEEQERLQKQKEEAEAKAREEAE-----RQRQEREKIMQQEEQ 130
PTZ00121 PTZ00121
MAEBL; Provisional
219-351 1.91e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 65.93  E-value: 1.91e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  219 DPIGEEERKQFAILAKIQAEEKqRRLDEAKEKLAIDKEK---LRLKKEALQRELEERNKAERQKKMDD-----EERHREK 290
Cdd:PTZ00121 1369 AEKKKEEAKKKADAAKKKAEEK-KKADEAKKKAEEDKKKadeLKKAAAAKKKADEAKKKAEEKKKADEakkkaEEAKKAD 1447
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392896888  291 ERQKKAERDARLQFAKENA--------AKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAER 351
Cdd:PTZ00121 1448 EAKKKAEEAKKAEEAKKKAeeakkadeAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAK 1516
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
174-357 3.13e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 64.96  E-value: 3.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  174 RQAQVRELFEHLANQTADKGKELRKFLSSILKEIHppedycikvyDPIGEEERKQFAILAKIQAEEKQRRLDEAKEKLAI 253
Cdd:COG1196   268 ELEELRLELEELELELEEAQAEEYELLAELARLEQ----------DIARLEERRRELEERLEELEEELAELEEELEELEE 337
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  254 DKEKLRLKKEALQRELEERNKAERQKK---MDDEERHREKERQKKAERDARLQFAKEnAAKLAAQEAKKDISLKSRLEQA 330
Cdd:COG1196   338 ELEELEEELEEAEEELEEAEAELAEAEealLEAEAELAEAEEELEELAEELLEALRA-AAELAAQLEELEEAEEALLERL 416
                         170       180
                  ....*....|....*....|....*..
gi 392896888  331 SMQQRERQKIDVQQAKLEAERILLLSK 357
Cdd:COG1196   417 ERLEEELEELEEALAELEEEEEEEEEA 443
PTZ00121 PTZ00121
MAEBL; Provisional
192-351 4.14e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 64.78  E-value: 4.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  192 KGKELRKflssiLKEIHPPEDYCIKVYDPIGEEERKQFAILAKIQAEEKQRRLDEAKEKLAIDKEKLRLKKEALQ----- 266
Cdd:PTZ00121 1291 KADEAKK-----AEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEaaeek 1365
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  267 RELEERNKAERQKKMDD-----EERHREKERQKKAERDARL--QFAKENAAKLAAQEAKKDISLKSRLEQASMQQRERQK 339
Cdd:PTZ00121 1366 AEAAEKKKEEAKKKADAakkkaEEKKKADEAKKKAEEDKKKadELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKK 1445
                         170
                  ....*....|..
gi 392896888  340 IDVQQAKLEAER 351
Cdd:PTZ00121 1446 ADEAKKKAEEAK 1457
PTZ00121 PTZ00121
MAEBL; Provisional
171-351 2.81e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 62.08  E-value: 2.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  171 QKYRQAQVRELFEHLANQTADKGKELRKflssiLKEIHPPEDycIKVYDPIGEEERKQFAILAKIQAEEKqRRLDEAKEK 250
Cdd:PTZ00121 1252 EEIRKFEEARMAHFARRQAAIKAEEARK-----ADELKKAEE--KKKADEAKKAEEKKKADEAKKKAEEA-KKADEAKKK 1323
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  251 laidKEKLRLKKEALQRELEERNKAERQKKMDDEERHREKERQKKAERDARLqfaKENAAKLAAQEAKKDISLKSRLEQA 330
Cdd:PTZ00121 1324 ----AEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEK---KKEEAKKKADAAKKKAEEKKKADEA 1396
                         170       180
                  ....*....|....*....|.
gi 392896888  331 SMQQRERQKIDVQQAKLEAER 351
Cdd:PTZ00121 1397 KKKAEEDKKKADELKKAAAAK 1417
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
223-355 6.63e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 60.72  E-value: 6.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  223 EEERKQfAILAKIQAEEKQRRLDEAKEKLAIDKEKLRLKKEALQRELEERNKAERQKKMDDEERHREKERQKKAERDARL 302
Cdd:COG1196   350 EEELEE-AEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 392896888  303 QFAKENAAKLAAQEAKKDI-SLKSRLEQASMQQRERQKIDVQQAKLEAERILLL 355
Cdd:COG1196   429 ALAELEEEEEEEEEALEEAaEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482
PTZ00121 PTZ00121
MAEBL; Provisional
171-352 6.98e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 60.54  E-value: 6.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  171 QKYRQAQVRELFEHLANQTADKGKELRKflSSILKEIhppedycikvydpigeeERKQFAILAKIQAEEKQRRLDEAKEK 250
Cdd:PTZ00121 1555 EELKKAEEKKKAEEAKKAEEDKNMALRK--AEEAKKA-----------------EEARIEEVMKLYEEEKKMKAEEAKKA 1615
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  251 laidkEKLRLKKEALQRELEERNKAERQKKMDDEERhREKERQKKAERDARLQFA----KENAAKLAAQEAKKDISLKSR 326
Cdd:PTZ00121 1616 -----EEAKIKAEELKKAEEEKKKVEQLKKKEAEEK-KKAEELKKAEEENKIKAAeeakKAEEDKKKAEEAKKAEEDEKK 1689
                         170       180
                  ....*....|....*....|....*.
gi 392896888  327 LEQASMQQRERQKIDVQQAKLEAERI 352
Cdd:PTZ00121 1690 AAEALKKEAEEAKKAEELKKKEAEEK 1715
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
223-351 7.25e-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: 59.09  E-value: 7.25e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   223 EEERKQFAILAKIQAEEKQRRLDEAKEKLAidKEKLRLKKEALQRELEERNK----AERQKKMDDEERHREKERQKKAER 298
Cdd:TIGR02794  108 EQAAKQAEEKQKQAEEAKAKQAAEAKAKAE--AEAERKAKEEAAKQAEEEAKakaaAEAKKKAEEAKKKAEAEAKAKAEA 185
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 392896888   299 DARlqfAKENAAKLAAQEAKKdislKSRLEQASMQQRERQKidvqQAKLEAER 351
Cdd:TIGR02794  186 EAK---AKAEEAKAKAEAAKA----KAAAEAAAKAEAEAAA----AAAAEAER 227
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
223-354 9.31e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.95  E-value: 9.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  223 EEERKQFAILAKI------------QAEEKQRRLDEAKEKLAIDK---EKLRLKKEALQRELEERNKAERQKKMDDEE-- 285
Cdd:COG1196   222 LKELEAELLLLKLreleaeleeleaELEELEAELEELEAELAELEaelEELRLELEELELELEEAQAEEYELLAELARle 301
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392896888  286 ---RHREKERQKKAERDARLQFAKENAAKLAAQEAKKDISLKSRLEQASMQQRERQK--IDVQQAKLEAERILL 354
Cdd:COG1196   302 qdiARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAelAEAEEALLEAEAELA 375
PTZ00121 PTZ00121
MAEBL; Provisional
224-346 1.48e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 59.77  E-value: 1.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  224 EERKQFAILAKIQAEEKqRRLDEAKEKLAIDKEKLRLKKEAlqrelEERNKAERQKKMDDEERHREkERQKKAERDARLQ 303
Cdd:PTZ00121 1414 AAAKKKADEAKKKAEEK-KKADEAKKKAEEAKKADEAKKKA-----EEAKKAEEAKKKAEEAKKAD-EAKKKAEEAKKAD 1486
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 392896888  304 FAKENA--AKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAK 346
Cdd:PTZ00121 1487 EAKKKAeeAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAE 1531
PTZ00121 PTZ00121
MAEBL; Provisional
171-350 1.55e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 59.38  E-value: 1.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  171 QKYRQAQVRELFEHLANQTADKGKELRKFLSSILKEIHP--PEDYCIKVYDPIGEEERKQFAILAKIQAEEKQRRLDEAK 248
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKlyEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKK 1640
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  249 EKLAIDKEKLRLKKEALQ---RELEERNKAERQKKMDDEERHREKERQKKAERDARlqfaKENAAKLAAQEAKKDISLKS 325
Cdd:PTZ00121 1641 KEAEEKKKAEELKKAEEEnkiKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKK----EAEEAKKAEELKKKEAEEKK 1716
                         170       180
                  ....*....|....*....|....*
gi 392896888  326 RLEQASMQQRERqKIDVQQAKLEAE 350
Cdd:PTZ00121 1717 KAEELKKAEEEN-KIKAEEAKKEAE 1740
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
224-351 2.00e-08

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: 57.62  E-value: 2.00e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   224 EERKQFAILAKIQAEEK-QRRLDEAKEKLaIDKEKLRLKKEALQRE--LEERNKAERQKKMDDE--------ERHREKER 292
Cdd:pfam13868   69 EERKRYRQELEEQIEEReQKRQEEYEEKL-QEREQMDEIVERIQEEdqAEAEEKLEKQRQLREEidefneeqAEWKELEK 147
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   293 QKKAERDAR-LQFAKENAAKLAAQEAKkdislksRLEQASMQQRERQKIDVQQAKLEAER 351
Cdd:pfam13868  148 EEEREEDERiLEYLKEKAEREEEREAE-------REEIEEEKEREIARLRAQQEKAQDEK 200
MAT1 pfam06391
CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for ...
234-359 2.01e-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: 55.71  E-value: 2.01e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   234 KIQAEEKQRRLDEAKE--KLAIDKEKLRLKKEalQRELEERNKAERQKKMD--DEERHREKERQKKAERDAR-----LQF 304
Cdd:pfam06391   60 GIDVEETEKKIEQYEKenKDLILKNKMKLSQE--EEELEELLELEKREKEErrKEEKQEEEEEKEKKEKAKQelideLMT 137
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392896888   305 AKENAAKLAAQEAKKDISLKSRLEQASM-------QQRERQKIDVQQAKLEAERILLLSKYP 359
Cdd:pfam06391  138 SNKDAEEIIAQHKKTAKKRKSERRRKLEelnrvleQKPTQFSTGIKFGQLPVPKIEEGPLYP 199
PTZ00121 PTZ00121
MAEBL; Provisional
223-350 2.23e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 59.00  E-value: 2.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  223 EEERKqfAILAKIQAEEKqRRLDEAKEKLAIDK--EKLRLKKEALQRELEERNKAERQKKMDDEERHREKERQ----KKA 296
Cdd:PTZ00121 1454 EEAKK--AEEAKKKAEEA-KKADEAKKKAEEAKkaDEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKadeaKKA 1530
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 392896888  297 ERDARLQFAKENAAKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAE 350
Cdd:PTZ00121 1531 EEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAE 1584
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
171-351 2.60e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.79  E-value: 2.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  171 QKYRQAQvRELFEHLANQTADKGKELRKFLSSILKEIHppedycikvydpigEEERKQFAILAKIQAEEKQrrLDEAKEK 250
Cdd:COG1196   213 ERYRELK-EELKELEAELLLLKLRELEAELEELEAELE--------------ELEAELEELEAELAELEAE--LEELRLE 275
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  251 LAIDKEKLRLKKEALQRELEERNKAERQKKMDDEERHREKERQKKAERD-ARLQFAKENAAKLAAQEAKKDISLKSRLE- 328
Cdd:COG1196   276 LEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEElAELEEELEELEEELEELEEELEEAEEELEe 355
                         170       180
                  ....*....|....*....|....
gi 392896888  329 -QASMQQRERQKIDVQQAKLEAER 351
Cdd:COG1196   356 aEAELAEAEEALLEAEAELAEAEE 379
PTZ00121 PTZ00121
MAEBL; Provisional
223-350 2.93e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 58.61  E-value: 2.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  223 EEERKqfAILAKIQAEEKQRRLDEAKEKLAIDKEKLRLKKEALQRELEERNKAERQKKMDDEERHREK---------ERQ 293
Cdd:PTZ00121 1480 EEAKK--ADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKkkadelkkaEEL 1557
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392896888  294 KKAERDARLQFAK-----ENAAKLAAQEAKKdiSLKSRLEQASMQQRERQKIDVQQAKLEAE 350
Cdd:PTZ00121 1558 KKAEEKKKAEEAKkaeedKNMALRKAEEAKK--AEEARIEEVMKLYEEEKKMKAEEAKKAEE 1617
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
223-339 3.42e-08

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 57.12  E-value: 3.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  223 EEERKQFAILAKIQAEEKQRRLDEAKEKLAIDKEKLRLKKEALQRELEERNKAE---RQKKMDDEERHREKERQKKAERD 299
Cdd:PRK09510  135 EEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEaeaAAKAAAEAKKKAEAEAKKKAAAE 214
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 392896888  300 ARLQFAKENAAKLAAQEAKKDISLKSRLEQASMQQRERQK 339
Cdd:PRK09510  215 AKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAK 254
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
224-353 7.64e-08

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: 56.08  E-value: 7.64e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   224 EERKQFaILAKIQAEEKQRRLDEAKEKLAIDKEKLRLKKEALQRELEERNKAERQKKMDDEERHREKERQKKAERD---A 300
Cdd:pfam13868  130 EEIDEF-NEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDelrA 208
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 392896888   301 RLQFA------KENAAKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAERIL 353
Cdd:pfam13868  209 KLYQEeqerkeRQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERML 267
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
248-350 1.00e-07

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 55.97  E-value: 1.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  248 KEKLAIDKEKLRLKKEALQ-RELEERNKAERQK-KMDDEERHREKERQKKAERDARLQFAKENAAKLAAQEAKKDISLKS 325
Cdd:PRK09510   70 QQKSAKRAEEQRKKKEQQQaEELQQKQAAEQERlKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKA 149
                          90       100       110
                  ....*....|....*....|....*....|...
gi 392896888  326 -----RLEQASMQQRE---RQKIDVQQAKLEAE 350
Cdd:PRK09510  150 eaeakRAAAAAKKAAAeakKKAEAEAAKKAAAE 182
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
223-350 1.21e-07

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: 55.24  E-value: 1.21e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   223 EEERKQFAILAKIQAEEKQRRLDEAKEKLAIDKEKLRLKKEALQRELEERNKAERQKKMDDEERHR--EKERQKKAERDA 300
Cdd:TIGR02794   61 PAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAkqAAEAKAKAEAEA 140
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 392896888   301 RLQfAKENAAKLAAQEAKKDislksRLEQASMQQRERQKIDVQQAKLEAE 350
Cdd:TIGR02794  141 ERK-AKEEAAKQAEEEAKAK-----AAAEAKKKAEEAKKKAEAEAKAKAE 184
PTZ00121 PTZ00121
MAEBL; Provisional
223-351 1.24e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 56.69  E-value: 1.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  223 EEERKqfAILAKIQAEEKqRRLDEAKEKLAIDKEKLRLKKEALQ-RELEE-RNKAERQKKMDDEERHREKERQK-----K 295
Cdd:PTZ00121 1441 EEAKK--ADEAKKKAEEA-KKAEEAKKKAEEAKKADEAKKKAEEaKKADEaKKKAEEAKKKADEAKKAAEAKKKadeakK 1517
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 392896888  296 AERDARLQFAKENAAKLAAQEAKK--DISLKSRLEQASMQQRERQKIDVQQAKLEAER 351
Cdd:PTZ00121 1518 AEEAKKADEAKKAEEAKKADEAKKaeEKKKADELKKAEELKKAEEKKKAEEAKKAEED 1575
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
223-351 1.52e-07

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: 54.92  E-value: 1.52e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   223 EEERKQFaiLAKIQAEEKQRRLDEAKEKLAIDK---EKLRLKKEALQRELEER---NKAERQKKMDDEERHREKERQKKA 296
Cdd:pfam13868   50 EEERERA--LEEEEEKEEERKEERKRYRQELEEqieEREQKRQEEYEEKLQEReqmDEIVERIQEEDQAEAEEKLEKQRQ 127
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 392896888   297 ERDARLQFAKENAAKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAER 351
Cdd:pfam13868  128 LREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEK 182
PTZ00121 PTZ00121
MAEBL; Provisional
223-346 1.72e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 56.30  E-value: 1.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  223 EEERKqfAILAKIQAEEKqRRLDEAKEKLAIDKEKLRLKKEA--------LQRELEERNKAERQKKMDDEERHREKERQK 294
Cdd:PTZ00121 1428 EEKKK--ADEAKKKAEEA-KKADEAKKKAEEAKKAEEAKKKAeeakkadeAKKKAEEAKKADEAKKKAEEAKKKADEAKK 1504
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 392896888  295 KAERDARLQFAKENAAKLAAQEAKKdISLKSRLEQASMQQRERQKIDVQQAK 346
Cdd:PTZ00121 1505 AAEAKKKADEAKKAEEAKKADEAKK-AEEAKKADEAKKAEEKKKADELKKAE 1555
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
221-357 1.72e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.10  E-value: 1.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  221 IGEEERKQFAILAKIQAEEKQRRLDEAKEKLAIDKEKLRLKKEALQRELEERNKAERQkkmddEERHREKERQKKAERDA 300
Cdd:COG1196   333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE-----ALRAAAELAAQLEELEE 407
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 392896888  301 RLQFAKENAAKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAERILLLSK 357
Cdd:COG1196   408 AEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL 464
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
223-350 1.91e-07

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: 54.85  E-value: 1.91e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   223 EEERKQFAILAKIQAEEKQRRLDE--AKEKLAIDKEKLRLKKEALQRELEE---RNKAERQKKMDDE-ERHREKERQKKA 296
Cdd:TIGR02794   73 LEQQAEEAEKQRAAEQARQKELEQraAAEKAAKQAEQAAKQAEEKQKQAEEakaKQAAEAKAKAEAEaERKAKEEAAKQA 152
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 392896888   297 ERDARLQFAKENAAKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAE 350
Cdd:TIGR02794  153 EEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAA 206
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
223-350 1.97e-07

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 54.81  E-value: 1.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  223 EEERKQFAILAKIQAEEKQRRLDEAKEKLAIDKEKLRLKKEAlQRELEERNKAERQKKMDDEERHREKERQKKAERDARL 302
Cdd:PRK09510   91 ELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQK-QAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKK 169
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 392896888  303 QfAKENAAKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAE 350
Cdd:PRK09510  170 K-AEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAK 216
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
224-350 3.02e-07

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 54.43  E-value: 3.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  224 EERKQFaiLAKIQAEEKQRRLDEAKEKL-AIDKEKLRLKKEALQRElEERNKAERQKKMDDEERHREKERQK-KAERDAR 301
Cdd:PRK09510   78 EEQRKK--KEQQQAEELQQKQAAEQERLkQLEKERLAAQEQKKQAE-EAAKQAALKQKQAEEAAAKAAAAAKaKAEAEAK 154
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 392896888  302 lqfAKENAAKLAAQEAKKdislKSRLEQASMQQRERQKIDVQQAKLEAE 350
Cdd:PRK09510  155 ---RAAAAAKKAAAEAKK----KAEAEAAKKAAAEAKKKAEAEAAAKAA 196
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
223-353 3.86e-07

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: 53.77  E-value: 3.86e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   223 EEERKQFAILAKIQAEEKQRRLDEAKEKLAIDKEKLRLKKEALQRELEERnkaERQKKMDDEERHREKERQKKAERDARL 302
Cdd:pfam13868   36 AEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEER---EQKRQEEYEEKLQEREQMDEIVERIQE 112
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 392896888   303 QFAKENAAKLAAQEAKKDIslksrLEQASMQQRERQKIDVQQAKLEAERIL 353
Cdd:pfam13868  113 EDQAEAEEKLEKQRQLREE-----IDEFNEEQAEWKELEKEEEREEDERIL 158
PTZ00121 PTZ00121
MAEBL; Provisional
188-352 4.06e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 54.76  E-value: 4.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  188 QTADKGKELRKFLSSILKEIHPPEDYCIKVYDPIGEEERKQfailAKIQAEEKQRRLDEAKeklaidKEKLRLKKEALQR 267
Cdd:PTZ00121 1240 EEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKA----DELKKAEEKKKADEAK------KAEEKKKADEAKK 1309
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  268 ELEERNKAERQKKMDDEERHREKERQKKAERDARlqfaKENAAKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKL 347
Cdd:PTZ00121 1310 KAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKK----AAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKK 1385

                  ....*
gi 392896888  348 EAERI 352
Cdd:PTZ00121 1386 KAEEK 1390
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
223-353 4.60e-07

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: 53.38  E-value: 4.60e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   223 EEERKQF-AILAKIQAEEKQRRLDEAKEKLAI---------DKEKLRLKKEALQRELEERNKAERQKKMDDEERHREKER 292
Cdd:pfam13868   97 LQEREQMdEIVERIQEEDQAEAEEKLEKQRQLreeidefneEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAERE 176
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392896888   293 QKKAERDARLQFAKENAAKLAAQEAKKDiSLKSRLEQASMQQRERQK-IDVQQAKLEAERIL 353
Cdd:pfam13868  177 EIEEEKEREIARLRAQQEKAQDEKAERD-ELRAKLYQEEQERKERQKeREEAEKKARQRQEL 237
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
223-348 4.77e-07

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: 53.38  E-value: 4.77e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   223 EEERKQFAILAKIQAEEKQRR--LDEAKEKLAIDkeklRLKKEALQRELEERNKAERQKKM-----DDEERHREKERQKK 295
Cdd:pfam13868  180 EEKEREIARLRAQQEKAQDEKaeRDELRAKLYQE----EQERKERQKEREEAEKKARQRQElqqarEEQIELKERRLAEE 255
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392896888   296 AERD--------ARLQFAKENAAKLAAQEAKKDISLKSRLEQAsMQQRERQKIDVQQAKLE 348
Cdd:pfam13868  256 AEREeeefermlRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQ-IEEREEQRAAEREEELE 315
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
171-350 5.86e-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: 5.86e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   171 QKYRQAQVRELFEHLANQTADKGKELRKFLSSILKEIhppedycikvyDPIGEEE---RKQFAILAKIQAEEKQRRLDEA 247
Cdd:pfam17380  412 QRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREM-----------ERVRLEEqerQQQVERLRQQEEERKRKKLELE 480
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   248 KEKLAiDKEKLRLKKEALQRELEERNKA----ERQKKM---DDEERHR---EKERQKKAERDARLQFAKENAAKLAaQEA 317
Cdd:pfam17380  481 KEKRD-RKRAEEQRRKILEKELEERKQAmieeERKRKLlekEMEERQKaiyEEERRREAEEERRKQQEMEERRRIQ-EQM 558
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 392896888   318 KKDISLKSRLEqASMQQRE--RQKIDVQQAKLEAE 350
Cdd:pfam17380  559 RKATEERSRLE-AMEREREmmRQIVESEKARAEYE 592
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
223-357 8.17e-07

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: 52.61  E-value: 8.17e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   223 EEERKQFAILAKIQAEEKQRRLDEAKEKLAIDKE-KLRLKKEALQRELEERNKAERQKKMDDEERHREKERQKKaerdAR 301
Cdd:pfam13868  213 EEQERKERQKEREEAEKKARQRQELQQAREEQIElKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRM----KR 288
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 392896888   302 LQFAKENAAKLAAQEAKKdisLKSRLEQASMQQRERQKIDVQQAKLEAERILLLSK 357
Cdd:pfam13868  289 LEHRRELEKQIEEREEQR---AAEREEELEEGERLREEEAERRERIEEERQKKLKE 341
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
222-359 1.21e-06

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: 50.07  E-value: 1.21e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   222 GEEERKQFAILAKIQAEEKQRRLDEAKEklaidkEKLRLKKEAlqRELEERNKAERQKKMDDEERHREKERQKKAERDAr 301
Cdd:pfam11600    9 SQEEKEKQRLEKDKERLRRQLKLEAEKE------EKERLKEEA--KAEKERAKEEARRKKEEEKELKEKERREKKEKDE- 79
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392896888   302 lqfaKENAAKLAAQEAK---KDISLKSRLEQASMQQRER----QKIDVQQAKLEAERILLLSKYP 359
Cdd:pfam11600   80 ----KEKAEKLRLKEEKrkeKQEALEAKLEEKRKKEEEKrlkeEEKRIKAEKAEITRFLQKPKTQ 140
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
232-349 1.22e-06

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


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 50.98  E-value: 1.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  232 LAKIQAEEKQ--RRLDEAKE---------KLAIDKEKLRLKKEALQRELEERNKAERQKKmddeerhrEKERQKKAERDA 300
Cdd:COG1842    46 LAQVIANQKRleRQLEELEAeaekweekaRLALEKGREDLAREALERKAELEAQAEALEA--------QLAQLEEQVEKL 117
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392896888  301 RLQfAKENAAKLAAQEAKKDIsLKSRLEQASMQQR-----------------ER--QKIDVQQAKLEA 349
Cdd:COG1842   118 KEA-LRQLESKLEELKAKKDT-LKARAKAAKAQEKvnealsgidsddatsalERmeEKIEEMEARAEA 183
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
221-364 1.47e-06

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 52.91  E-value: 1.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  221 IGEEERKQFAILAKiqAEEKQRRLDEAKEKLAIDKEKLRLKKEALQRELEERNKAERQKKMDDEERHREKERQKKAERDA 300
Cdd:PRK00409  511 IGEDKEKLNELIAS--LEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADE 588
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392896888  301 RLQFAKE-NAAKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKL--EAERIlllsKYPNFG-KG 364
Cdd:PRK00409  589 IIKELRQlQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEElkVGDEV----KYLSLGqKG 652
Nop53 pfam07767
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ...
223-341 2.01e-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: 2.01e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   223 EEERKqfailaKIQAEEKQRRLDEAKEKLAIDKEKLRLKKEALQreleERNKAErqkkmddeeRHREKERQKKAERDARL 302
Cdd:pfam07767  206 EAEKK------RLKEEEKLERVLEKIAESAATAEAREEKRKTKA----QRNKEK---------RRKEEEREAKEEKALKK 266
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 392896888   303 QFAK-ENAAKLAAQEAKKDISLKSRLEQASMQQRERQKID 341
Cdd:pfam07767  267 KLAQlERLKEIAKEIAEKEKEREEKAEARKREKRKKKKEE 306
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
191-350 2.20e-06

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


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 51.93  E-value: 2.20e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   191 DKGKELRKFLSSiLKEIHPPEDycikvydpigeEERKQfaiLAKIQAEEKQRRLDEAKEKLAIDKEKL-RLKKEALQREL 269
Cdd:pfam05262  191 EKGVNFRRDMTD-LKERESQED-----------AKRAQ---QLKEELDKKQIDADKAQQKADFAQDNAdKQRDEVRQKQQ 255
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   270 EERN---KAERQKKMDD----EERHREKER-QKKAER-DARLQFAKENAAKLAAQEAKkdiSLKSRLEQASMQ-QRERQK 339
Cdd:pfam05262  256 EAKNlpkPADTSSPKEDkqvaENQKREIEKaQIEIKKnDEEALKAKDHKAFDLKQESK---ASEKEAEDKELEaQKKREP 332
                          170
                   ....*....|...
gi 392896888   340 I--DVQQAKLEAE 350
Cdd:pfam05262  333 VaeDLQKTKPQVE 345
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
238-354 2.73e-06

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: 48.50  E-value: 2.73e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   238 EEKQRRLDEAKEklaidkeklRLKKEALQRELEERNKAERQKKMDDEERHR--EKERQKKAERdarlQFAKENAAKLAAQ 315
Cdd:pfam05672   17 AEKRRQAREQRE---------REEQERLEKEEEERLRKEELRRRAEEERARreEEARRLEEER----RREEEERQRKAEE 83
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 392896888   316 EAKKDisLKSRLEQASMQQRERQKIDVqQAKLEAERILL 354
Cdd:pfam05672   84 EAEER--EQREQEEQERLQKQKEEAEA-KAREEAERQRQ 119
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
234-350 2.99e-06

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 50.96  E-value: 2.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  234 KIQAEEK-QRRLDEAKEKLAIDK-EKLRLKKEALQREL----EERNKAERQKKMDDEERHREKERQKKAERDARLQFAK- 306
Cdd:PRK09510   66 RQQQQQKsAKRAEEQRKKKEQQQaEELQQKQAAEQERLkqleKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAa 145
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 392896888  307 ----ENAAKLAAQEAKKDISLKSRLEQASMQQRERQKidvQQAKLEAE 350
Cdd:PRK09510  146 kakaEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAE---AKKKAEAE 190
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
223-326 3.05e-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: 51.49  E-value: 3.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   223 EEERKQFAIL------AKIQAEEKQRRLDEAKEKLAIDKEKLRLKKEALQRELEERnKAERQKK---MDDEERHREKERQ 293
Cdd:pfam15709  405 EEERKQRLQLqaaqerARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQ-LAEEQKRlmeMAEEERLEYQRQK 483
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 392896888   294 KKAERDARLQFAK-----ENAAKLAAQEAKKDISLKSR 326
Cdd:pfam15709  484 QEAEEKARLEAEErrqkeEEAARLALEEAMKQAQEQAR 521
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
223-383 3.21e-06

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


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 51.19  E-value: 3.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  223 EEERKQfailAKIQAEeKQRRLDEAKEKLAIDKEKLRLKKEALQRELEErnKAERQKKMDDEERHREKERQKKAERDARL 302
Cdd:COG3064    63 EAEQRA----AELAAE-AAKKLAEAEKAAAEAEKKAAAEKAKAAKEAEA--AAAAEKAAAAAEKEKAEEAKRKAEEEAKR 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  303 QFAKE--NAAKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAERILLLSKYPNFGKGPTAAAATRPQVTAKQV 380
Cdd:COG3064   136 KAEEErkAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAA 215

                  ...
gi 392896888  381 PLN 383
Cdd:COG3064   216 LLA 218
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
223-351 3.42e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.86  E-value: 3.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  223 EEERKQFAILAKIQAEEKQRRLDEAKEKLAidkEKLRLKKEALQRELEERNKA-----ERQKKMDDEERHREKERQKKAE 297
Cdd:COG1196   339 LEELEEELEEAEEELEEAEAELAEAEEALL---EAEAELAEAEEELEELAEELlealrAAAELAAQLEELEEAEEALLER 415
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 392896888  298 RDARLQFAKENAAKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAER 351
Cdd:COG1196   416 LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
223-351 4.11e-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: 4.11e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   223 EEERKQfailaKIQAEEKQRRLDEAK-EKLAIDKEKLRLKKEALQRELEERNKAERQKKMDDEERHREKERQKKAERDAR 301
Cdd:pfam17380  399 EAARKV-----KILEEERQRKIQQQKvEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERK 473
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392896888   302 ---LQFAKENAAKLAAQEAKKDI---SLKSRlEQASMQQRERQKI------DVQQAKLEAER 351
Cdd:pfam17380  474 rkkLELEKEKRDRKRAEEQRRKIlekELEER-KQAMIEEERKRKLlekemeERQKAIYEEER 534
PTZ00121 PTZ00121
MAEBL; Provisional
223-351 4.60e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.30  E-value: 4.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  223 EEERKQFAILAKiQAEEKQRRLDEAKEKLAIDK---EKLRLKKEALQRELEERNKAERQKKMDDEERHREKERQKKAERD 299
Cdd:PTZ00121 1670 AEEDKKKAEEAK-KAEEDEKKAAEALKKEAEEAkkaEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEE 1748
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 392896888  300 ARLQFAKEN-AAKLAAQEAKKdiSLKSRLEQASMQQRERQKIDvQQAKLEAER 351
Cdd:PTZ00121 1749 AKKDEEEKKkIAHLKKEEEKK--AEEIRKEKEAVIEEELDEED-EKRRMEVDK 1798
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
236-350 6.38e-06

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 50.26  E-value: 6.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  236 QAEEKQRRLDEAKEKLAIDKEKlRLKKEALQRElEERNKAERQKKMDDEERHREKERQK-----KAERDARLQfakENAA 310
Cdd:COG2268   225 EAELEQEREIETARIAEAEAEL-AKKKAEERRE-AETARAEAEAAYEIAEANAEREVQRqleiaEREREIELQ---EKEA 299
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 392896888  311 KLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAE 350
Cdd:COG2268   300 EREEAELEADVRKPAEAEKQAAEAEAEAEAEAIRAKGLAE 339
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
236-351 7.73e-06

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


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 50.04  E-value: 7.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  236 QAEEKQRRLDEAKEKLAIDKEKLRLKKEALQRELEERNKaERQKKMDDEERHREKERQKKAERDARLQFAKENAAK--LA 313
Cdd:COG3064     3 EALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEE-ERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKklAE 81
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 392896888  314 AQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAER 351
Cdd:COG3064    82 AEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEK 119
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
238-351 8.92e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.32  E-value: 8.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  238 EEKQRRLDEAKEKLAidkeklRLkkEALQRELE--------ERNKAERQKKMDDEERHREKERQKKAERDARLQFAKENA 309
Cdd:COG1196   175 EEAERKLEATEENLE------RL--EDILGELErqleplerQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEA 246
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 392896888  310 AKLAAQEAKKDISLKSRLEQASMQQrERQKIDVQQAKLEAER 351
Cdd:COG1196   247 ELEELEAELEELEAELAELEAELEE-LRLELEELELELEEAQ 287
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
160-353 9.47e-06

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 50.36  E-value: 9.47e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   160 VREMDHCIYWIQKY-RQAQVRELFEHLANQTADKGKELRKFLSSILKE---IHPPEDYCIKVYDPIGEEERKQFaILAKI 235
Cdd:pfam02463  229 LDYLKLNEERIDLLqELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEeekEKKLQEEELKLLAKEEEELKSEL-LKLER 307
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   236 QAEEKQRRLDEAKEKLA-IDKEKLRLKKEALQRELE----ERNKAERQKKMDDEERHREKERQKKAERDARL----QFAK 306
Cdd:pfam02463  308 RKVDDEEKLKESEKEKKkAEKELKKEKEEIEELEKElkelEIKREAEEEEEEELEKLQEKLEQLEEELLAKKklesERLS 387
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 392896888   307 ENAAKLAAQEAKKDISLKSRLEQasMQQRERQKIDVQQAKLEAERIL 353
Cdd:pfam02463  388 SAAKLKEEELELKSEEEKEAQLL--LELARQLEDLLKEEKKEELEIL 432
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
224-405 1.28e-05

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


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 49.27  E-value: 1.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  224 EERKQFAILAKIQAEEKQRR----LDEAKEKLAIDKEKLRLKKEALQRELEERNKAERQKKMDDEERHREKERQKKAERD 299
Cdd:COG3064    40 EEERLAELEAKRQAEEEAREakaeAEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEK 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  300 ARLQFAKENA---AKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAERILLLSKYPNFGKGPTAAAATRPQVT 376
Cdd:COG3064   120 EKAEEAKRKAeeeAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAA 199
                         170       180
                  ....*....|....*....|....*....
gi 392896888  377 AKQVPLNPYGVSSFGVAQAIIVPDNNAQR 405
Cdd:COG3064   200 AAALAAAAAAAAADAALLALAVAARAAAA 228
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
234-357 1.29e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.94  E-value: 1.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  234 KIQAEEKQRRLDEAKekLAIDKEKLRLKKEALQRELEERNKAERQKKMDDEERHREKERQKKAERDARLqfakeNAAKLA 313
Cdd:COG1196   217 ELKEELKELEAELLL--LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL-----EEAQAE 289
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 392896888  314 AQEAKKDISlksRLEQASMQQRERQK-IDVQQAKLEAERILLLSK 357
Cdd:COG1196   290 EYELLAELA---RLEQDIARLEERRReLEERLEELEEELAELEEE 331
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
223-377 1.50e-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: 49.68  E-value: 1.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   223 EEERKQFAILAKIQAEEKQRRldeakEKLAIDKEKLrLKKEALQRELEER---------NKAERQKK-----MDDEERHR 288
Cdd:TIGR02169  180 EEVEENIERLDLIIDEKRQQL-----ERLRREREKA-ERYQALLKEKREYegyellkekEALERQKEaierqLASLEEEL 253
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   289 EK---ERQKKAER-DARLQFAKENAAKLAAQ------EAKKDI-SLKSRLEQA----SMQQRERQKIDVQQAKLEAERIL 353
Cdd:TIGR02169  254 EKlteEISELEKRlEEIEQLLEELNKKIKDLgeeeqlRVKEKIgELEAEIASLersiAEKERELEDAEERLAKLEAEIDK 333
                          170       180
                   ....*....|....*....|....
gi 392896888   354 LLSKYPNFGKGPTAAAATRPQVTA 377
Cdd:TIGR02169  334 LLAEIEELEREIEEERKRRDKLTE 357
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
179-349 1.61e-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: 49.68  E-value: 1.61e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   179 RELFEHLAN-QTADKGKE-LRKFLSSILKEIHPPEDYCIKVYDPIGEEERKQFAILAKIQA--EEKQRRLDEAKEKLAID 254
Cdd:TIGR02169  223 YEGYELLKEkEALERQKEaIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDlgEEEQLRVKEKIGELEAE 302
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   255 KEKLRLKKEALQRELEErnkAERQKKMDDEERHREKERQKKAERDARlQFAKENAAKLAAQEAKKDI--SLKSRLEQASM 332
Cdd:TIGR02169  303 IASLERSIAEKERELED---AEERLAKLEAEIDKLLAEIEELEREIE-EERKRRDKLTEEYAELKEEleDLRAELEEVDK 378
                          170
                   ....*....|....*...
gi 392896888   333 QQRE-RQKIDVQQAKLEA 349
Cdd:TIGR02169  379 EFAEtRDELKDYREKLEK 396
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
233-399 1.88e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 48.67  E-value: 1.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  233 AKIQAEEKQRRLDEAKEKLAIDKEKLRLKKEALQREleernKAERQKKMDDEERHREKERQKKAERDARLQfAKENAAKL 312
Cdd:COG3883   141 DKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ-----QAEQEALLAQLSAEEAAAEAQLAELEAELA-AAEAAAAA 214
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  313 AAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAERILLLSKYPNFGKGPTAAAATRPQVTAKQVPLNPYGVSSFGV 392
Cdd:COG3883   215 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGG 294

                  ....*..
gi 392896888  393 AQAIIVP 399
Cdd:COG3883   295 GGGAASG 301
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
238-351 2.03e-05

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: 45.29  E-value: 2.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   238 EEKQRRLDEAKEKLAIDKEKLRLKKEALQRELEERNKAERQKKMDDEERHR-EKERQKKAERDARLQFAKENAAK----L 312
Cdd:pfam20492    2 EEAEREKQELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERlEQKRQEAEEEKERLEESAEMEAEekeqL 81
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 392896888   313 AAQEAKKDiSLKSRLEQASmqqrERQKIDVQQAKLEAER 351
Cdd:pfam20492   82 EAELAEAQ-EEIARLEEEV----ERKEEEARRLQEELEE 115
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
223-350 2.15e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 48.36  E-value: 2.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  223 EEERKQFAILAKIQAE--EKQRRLDEAKEKLAIDKEKLRLKK---EALQRELEERNK--AERQKKMDDEERHREKERQKK 295
Cdd:COG4372    31 EQLRKALFELDKLQEEleQLREELEQAREELEQLEEELEQARselEQLEEELEELNEqlQAAQAELAQAQEELESLQEEA 110
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 392896888  296 AERDARLQFAKENAAKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAE 350
Cdd:COG4372   111 EELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
229-357 2.35e-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: 47.99  E-value: 2.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   229 FAILAKIQAEEKQRRLDEAKEKLAIDK--EKLRLKKEALQRELEERNKAERQK-KMDDEERHREKERQKKAERDARLQFA 305
Cdd:pfam13868   21 NKERDAQIAEKKRIKAEEKEEERRLDEmmEEERERALEEEEEKEEERKEERKRyRQELEEQIEEREQKRQEEYEEKLQER 100
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 392896888   306 KENAAKLAAQEAKkdislksrlEQASMQQRERQKIDVQQAKLEAERILLLSK 357
Cdd:pfam13868  101 EQMDEIVERIQEE---------DQAEAEEKLEKQRQLREEIDEFNEEQAEWK 143
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
233-354 2.37e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 48.36  E-value: 2.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  233 AKIQAEEKQRRLDEAKEKLAIDKEKLRLKKEALQRELEERNKAERQkkMDDEERHREKERQKKAERDARLQFAKENAAKL 312
Cdd:COG4372    57 AREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEE--LESLQEEAEELQEELEELQKERQDLEQQRKQL 134
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 392896888  313 AAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAERILL 354
Cdd:COG4372   135 EAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAL 176
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
167-358 2.44e-05

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: 48.81  E-value: 2.44e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   167 IYWIQKY-RQAQVRELFEHLANQTADKGKELRKFLSSILKEIHPPEDYCIKVYdpigEEERKQFAILAKI-QAEEKQRRL 244
Cdd:pfam02463  166 RLKRKKKeALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEK----LELEEEYLLYLDYlKLNEERIDL 241
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   245 DEAK-----EKLAIDKEKLRLKKEALQRELEERNKAERQKKMDDEER-----HREKERQKKAERDARLQFAKENAAKLAA 314
Cdd:pfam02463  242 LQELlrdeqEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELkllakEEEELKSELLKLERRKVDDEEKLKESEK 321
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 392896888   315 QEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAERILLLSKY 358
Cdd:pfam02463  322 EKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQ 365
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
220-362 2.71e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.52  E-value: 2.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  220 PIGEEERKQfaILAKIQAEEKqrRLDEAKEKLAIDKEKLRLKKEALQRELEERNKAERQKKMDDEERHREKERQK----K 295
Cdd:PRK03918  444 ELTEEHRKE--LLEEYTAELK--RIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKynleE 519
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392896888  296 AERDAR-LQFAKENAAKLaaqeaKKDI-SLKSRLEQASMQQRERQKIDVQQAKLEAERILLLSKYPNFG 362
Cdd:PRK03918  520 LEKKAEeYEKLKEKLIKL-----KGEIkSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELG 583
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
223-309 2.71e-05

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: 44.91  E-value: 2.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   223 EEERKQfailakiqAEEKQRRLDEAKEKLAIDKEKLRLKKEalqRELEERNKAERQKKMDDEERHR-EKERQKKAERDAR 301
Cdd:pfam20492   40 EEERRQ--------AEEEAERLEQKRQEAEEEKERLEESAE---MEAEEKEQLEAELAEAQEEIARlEEEVERKEEEARR 108

                   ....*...
gi 392896888   302 LQFAKENA 309
Cdd:pfam20492  109 LQEELEEA 116
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
223-350 2.74e-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: 48.41  E-value: 2.74e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   223 EEERKQfailakiqAEEKQRRLDEAKEKLAID----KEKLRLKK-----EALQRELEERNKAeRQKKMDDEERHREKE-- 291
Cdd:pfam15709  358 EEQRRL--------QQEQLERAEKMREELELEqqrrFEEIRLRKqrleeERQRQEEEERKQR-LQLQAAQERARQQQEef 428
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392896888   292 RQKKAERDARLQfakENAAKLAAQEAKKDISLKSRLEQAS---MQQRERQKIDVQQAKLEAE 350
Cdd:pfam15709  429 RRKLQELQRKKQ---QEEAERAEAEKQRQKELEMQLAEEQkrlMEMAEEERLEYQRQKQEAE 487
MT pfam12777
Microtubule-binding stalk of dynein motor; the 380 kDa motor unit of dynein belongs to the AAA ...
232-317 3.16e-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: 47.76  E-value: 3.16e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   232 LAKIQAEEKQrrLDEAKEKLAIDKEKLRLKKEALQRELE----ERNKAERQKKMDDEERHRE-------KERQKKAERDa 300
Cdd:pfam12777    7 LLKLHSTAAQ--VDDLKAKLAAQEAELKQKNEDADKLIQvvgiEADKVSKEKAIADEEEQKVavimkevKEKQKACEED- 83
                           90
                   ....*....|....*..
gi 392896888   301 rlqFAKENAAKLAAQEA 317
Cdd:pfam12777   84 ---LAKAEPALLAAQAA 97
PTZ00121 PTZ00121
MAEBL; Provisional
171-351 3.36e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.60  E-value: 3.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  171 QKYRQAQVRELFEHLANQTADKGKELRKFLSSILK--EIHPPEDYciKVYDPIGEEERKQFAILAKiQAEEKQRRlDEAK 248
Cdd:PTZ00121 1477 KKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKadEAKKAEEA--KKADEAKKAEEAKKADEAK-KAEEKKKA-DELK 1552
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  249 EklaidKEKLRLKKEalQRELEERNKAERQKKMddEERHREKERQKKAERDARLQFAKENAAKLAAQEAKKDISLKSRLE 328
Cdd:PTZ00121 1553 K-----AEELKKAEE--KKKAEEAKKAEEDKNM--ALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAE 1623
                         170       180
                  ....*....|....*....|...
gi 392896888  329 QASMQQRERQKIDVQQAKLEAER 351
Cdd:PTZ00121 1624 ELKKAEEEKKKVEQLKKKEAEEK 1646
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
156-351 3.73e-05

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 48.25  E-value: 3.73e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   156 LESHVREMDHCIYWIQ---KYRQAQVRELFEHLANQTADKGK-ELRKF-LSSILKEIHppEDYCIKvydpigEEERkqfa 230
Cdd:pfam01576   80 LESRLEEEEERSQQLQnekKKMQQHIQDLEEQLDEEEAARQKlQLEKVtTEAKIKKLE--EDILLL------EDQN---- 147
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   231 ilAKIQAEEKQ--RRLDEAKEKLAIDKEK------LRLKKEALQRELEERNKAERQKKMDDEERHREKERQKKAERD--A 300
Cdd:pfam01576  148 --SKLSKERKLleERISEFTSNLAEEEEKakslskLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEqiA 225
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392896888   301 RLQfakENAAKLAAQEAKKDISLKS---RLEQASMQQRERQK--------IDVQQAKLEAER 351
Cdd:pfam01576  226 ELQ---AQIAELRAQLAKKEEELQAalaRLEEETAQKNNALKkireleaqISELQEDLESER 284
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
234-354 4.17e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.01  E-value: 4.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  234 KIQAEeKQRRLDEAKEKL-AIDKEKLRLKKEALQRELE---------ERNKAERQKKMDDEERHREKERQKKAERDARLQ 303
Cdd:COG1196   206 ERQAE-KAERYRELKEELkELEAELLLLKLRELEAELEeleaeleelEAELEELEAELAELEAELEELRLELEELELELE 284
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 392896888  304 FAKENAAKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAERILL 354
Cdd:COG1196   285 EAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEEL 335
RRP36 pfam06102
rRNA biogenesis protein RRP36; RRP36 is involved in the early processing steps of the pre-rRNA.
226-325 4.59e-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: 45.24  E-value: 4.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   226 RKQFAILAKIQAEEKQrrldEAKEKLaiDKEKLRLKKEALQRELEERNKAERQKKMDDEERHREKERqKKAERDARLQ-- 303
Cdd:pfam06102   48 RKNYGFLDEYRKKEIE----ELKKQL--KKTKDPEEKEELKRTLQSMESRLKAKKRKDREREVLKEH-KKEEKEKVKQgk 120
                           90       100
                   ....*....|....*....|....*
gi 392896888   304 ---FAKENAAKLAAQEAKKDiSLKS 325
Cdd:pfam06102  121 kpfYLKKSEKKKLLLKEKFE-ELKK 144
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
171-357 5.14e-05

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: 48.04  E-value: 5.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   171 QKYRQAQVRELF-----EHLANQTADKGKELRKFLSSILKEIHPPEDYCIKVYDPIGEEE----RKQFAILAKIQAEEKQ 241
Cdd:pfam02463  300 SELLKLERRKVDdeeklKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEelekLQEKLEQLEEELLAKK 379
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   242 RRLDEAKEKLAIDKEKLRLKKEALQRELEERNKAERQKKMDDEERHREKERQKKAERDaRLQFAKENAAKLAAQEAKKDI 321
Cdd:pfam02463  380 KLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEE-SIELKQGKLTEEKEELEKQEL 458
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 392896888   322 SLKSRLEQASMQQRERQKIDVQQAKLEAERILLLSK 357
Cdd:pfam02463  459 KLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQK 494
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
232-352 5.47e-05

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: 45.83  E-value: 5.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   232 LAKIQAEEKQ--RRLDEAKEKLAIDKEK----LRLKKEALQRE-LEERNKAERQKkmddEERHREKERQKKAERDARLQF 304
Cdd:pfam04012   45 LAQTIARQKQleRRLEQQTEQAKKLEEKaqaaLTKGNEELAREaLAEKKSLEKQA----EALETQLAQQRSAVEQLRKQL 120
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 392896888   305 AKeNAAKLAAQEAKKDIsLKSRLEQASMQQ---RERQKIDVQQAKLEAERI 352
Cdd:pfam04012  121 AA-LETKIQQLKAKKNL-LKARLKAAKAQEavqTSLGSLSTSSATDSFERI 169
PTZ00121 PTZ00121
MAEBL; Provisional
238-360 6.27e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.83  E-value: 6.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  238 EEKQRRLDEAKEKLAIDKEKLRLKKEALQRElEERNKAERQKKMDDEerhREKERQKKAERDARLQFAKENAAKLAAQEA 317
Cdd:PTZ00121 1094 EEAFGKAEEAKKTETGKAEEARKAEEAKKKA-EDARKAEEARKAEDA---RKAEEARKAEDAKRVEIARKAEDARKAEEA 1169
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 392896888  318 KKDISLKsRLEQASMQQRERQKIDVQQAKlEAERILLLSKYPN 360
Cdd:PTZ00121 1170 RKAEDAK-KAEAARKAEEVRKAEELRKAE-DARKAEAARKAEE 1210
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
222-349 6.28e-05

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: 46.42  E-value: 6.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  222 GEEERKQFaiLAKIQAEEKQ-RRLDEAKEKLAIDKEKLRLKKEAL---QRELEERNKAERQKKMDDEERHREKERQ--KK 295
Cdd:cd16269   168 AEEVLQEF--LQSKEAEAEAiLQADQALTEKEKEIEAERAKAEAAeqeRKLLEEQQRELEQKLEDQERSYEEHLRQlkEK 245
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 392896888  296 AERDARLQfakenaaklaAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEA 349
Cdd:cd16269   246 MEEERENL----------LKEQERALESKLKEQEALLEEGFKEQAELLQEEIRS 289
CCDC47 pfam07946
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ...
253-339 6.74e-05

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: 46.41  E-value: 6.74e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   253 IDK--EKLRLKKEALQR-------ELEERNKAERQKKMddEERHREKERQKKAERDARLqfakenaAKLAAQEAKKdisl 323
Cdd:pfam07946  245 IDKlaKRAKLRPEALKKakktreeEIEKIKKAAEEERA--EEAQEKKEEAKKKEREEKL-------AKLSPEEQRK---- 311
                           90
                   ....*....|....*.
gi 392896888   324 ksrleqasMQQRERQK 339
Cdd:pfam07946  312 --------YEEKERKK 319
DDRGK pfam09756
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ...
248-338 7.23e-05

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: 45.03  E-value: 7.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   248 KEKLAIdKEKLRLKKEALQRELEERNK--AERQKKMDDEERHREKERQKKAERDARLQFAKENAAKLAAQEAKKDISLKS 325
Cdd:pfam09756    8 RAKLEL-KEAKRQQREAEEEEREEREKleEKREEEYKEREEREEEAEKEKEEEERKQEEEQERKEQEEYEKLKSQFVVEE 86
                           90
                   ....*....|...
gi 392896888   326 RLEQASMQQRERQ 338
Cdd:pfam09756   87 EGTDKLSAEDESQ 99
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
151-351 7.25e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 47.37  E-value: 7.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  151 KRAIALESHVREMDHciywiqkyrqaQVRELFEHLAN---QTADKGKELRKFLSSILKEIHPPEDYCIKVYDpigeeerk 227
Cdd:PRK03918  549 EKLEELKKKLAELEK-----------KLDELEEELAEllkELEELGFESVEELEERLKELEPFYNEYLELKD-------- 609
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  228 qfailAKIQAEEKQRRLDEAKEKLAIDKEKLRLKKEALqRELeeRNKAERQKKMDDEERHREKERQ--KKAERDARLQFA 305
Cdd:PRK03918  610 -----AEKELEREEKELKKLEEELDKAFEELAETEKRL-EEL--RKELEELEKKYSEEEYEELREEylELSRELAGLRAE 681
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 392896888  306 KENAAKLaAQEAKKDIS-LKSRLEQASMQQRERQKIDVQQAKLEAER 351
Cdd:PRK03918  682 LEELEKR-REEIKKTLEkLKEELEEREKAKKELEKLEKALERVEELR 727
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
236-404 7.33e-05

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


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 46.96  E-value: 7.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  236 QAEEKQRRLDEAKEKLAIDKEKLRLKKEALQRELEE---RNKAERQKKMDDEERHREKERQKKAERDARLQFAKENAAKL 312
Cdd:COG3064    20 QAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEearEAKAEAEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAK 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  313 AAQEAKKDISLKSRLEQASMQQRERQKIDVQQ-AKLEAERILLLSKYPNFGKGPTAAAATRPQVTAKQVPLNPYGVSSFG 391
Cdd:COG3064   100 AAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEeAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAA 179
                         170
                  ....*....|...
gi 392896888  392 VAQAIIVPDNNAQ 404
Cdd:COG3064   180 AALVAAAAAAVEA 192
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
238-319 9.09e-05

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: 44.27  E-value: 9.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   238 EEKQRRLDEAKEKL------AIDKEKLRLKKEALQRELEERNK--------AERQKKMDDEERHREKERQKKAERDARLq 303
Cdd:pfam15346   37 AEVERRVEEARKIMekqvleELEREREAELEEERRKEEEERKKreelerilEENNRKIEEAQRKEAEERLAMLEEQRRM- 115
                           90
                   ....*....|....*.
gi 392896888   304 faKENAAKLAAQEAKK 319
Cdd:pfam15346  116 --KEERQRREKEEEER 129
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
223-303 9.30e-05

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: 44.26  E-value: 9.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   223 EEERKQFAILAKIQAEEKQRRLDEAK-----EKLAIDKEKLRLKKEALQRELEERNKAERQKKMDDE---------ERHR 288
Cdd:pfam05672   39 EEERLRKEELRRRAEEERARREEEARrleeeRRREEEERQRKAEEEAEEREQREQEEQERLQKQKEEaeakareeaERQR 118
                           90
                   ....*....|....*.
gi 392896888   289 -EKERQKKAERDARLQ 303
Cdd:pfam05672  119 qEREKIMQQEEQERLE 134
CCDC66 pfam15236
Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil ...
226-339 9.71e-05

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: 44.02  E-value: 9.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   226 RKQFAILAKIQAEEKQRRLDEAKEKLAIDKEKLRLKKeaLQRELEErnkaERQKKMDDEE-----RHREKErQKKAERDA 300
Cdd:pfam15236   33 RGQNALLDPAQLEERERKRQKALEHQNAIKKQLEEKE--RQKKLEE----ERRRQEEQEEeerlrREREEE-QKQFEEER 105
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 392896888   301 RLQFAKENAAKLAAQEakkdisLKSRLEQASMQ-QRERQK 339
Cdd:pfam15236  106 RKQKEKEEAMTRKTQA------LLQAMQKAQELaQRLKQE 139
PTZ00121 PTZ00121
MAEBL; Provisional
223-350 9.89e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 9.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  223 EEERKQFAI--LAKIQAEEKQRRLDEAKEKLAIDK-EKLRLKKEAlqRELEERNKAERQKKMDDEERHREKERQKKAER- 298
Cdd:PTZ00121 1179 EAARKAEEVrkAEELRKAEDARKAEAARKAEEERKaEEARKAEDA--KKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRk 1256
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 392896888  299 --DARLQFAKENAAKLAAQEAKKDISLKSRLE--QASMQQRERQKIDVQQAKLEAE 350
Cdd:PTZ00121 1257 feEARMAHFARRQAAIKAEEARKADELKKAEEkkKADEAKKAEEKKKADEAKKKAE 1312
PRK12704 PRK12704
phosphodiesterase; Provisional
223-356 1.10e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 46.31  E-value: 1.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  223 EEERKQFAILAKIQAEE-KQRRLDEAKEKlaIDKEKLRLKKEA--------------LQRE---------LEERNKAERQ 278
Cdd:PRK12704   37 EEEAKRILEEAKKEAEAiKKEALLEAKEE--IHKLRNEFEKELrerrnelqklekrlLQKEenldrklelLEKREEELEK 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  279 KKMDDEERHRE-KERQKKAERDARLQFAK-ENAAKLAAQEAKKDI--SLKSRLE-QASMQQRERQKIDVQQAKLEAERIL 353
Cdd:PRK12704  115 KEKELEQKQQElEKKEEELEELIEEQLQElERISGLTAEEAKEILleKVEEEARhEAAVLIKEIEEEAKEEADKKAKEIL 194

                  ...
gi 392896888  354 LLS 356
Cdd:PRK12704  195 AQA 197
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
223-333 1.20e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 45.95  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  223 EEERKQFAILAKIQAEEKQRRLDEAKEKLAIDKEKLRLKKEALQR---ELEERNKAERQKKMDDEERhrekerqKKAERD 299
Cdd:PRK09510  150 EAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKaaaEAKKKAEAEAKKKAAAEAK-------KKAAAE 222
                          90       100       110
                  ....*....|....*....|....*....|....
gi 392896888  300 ARLQFAKENAAKLAAQEAKKDISLKSRLEQASMQ 333
Cdd:PRK09510  223 AKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAA 256
PTZ00121 PTZ00121
MAEBL; Provisional
188-351 1.47e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.67  E-value: 1.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  188 QTADKGKELRKflssiLKEIHPPEDycIKVYDPIGEEERKQFAILAKIQAEEKQRRLDEAKEKLAIdkEKLRLKKEALQR 267
Cdd:PTZ00121 1531 EEAKKADEAKK-----AEEKKKADE--LKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKA--EEARIEEVMKLY 1601
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  268 ELEERNKAERQKKMDD-----EERHREKERQKKAERDAR-----------LQFAKENAAKLAAQEAKKDISLKSRLEQAS 331
Cdd:PTZ00121 1602 EEEKKMKAEEAKKAEEakikaEELKKAEEEKKKVEQLKKkeaeekkkaeeLKKAEEENKIKAAEEAKKAEEDKKKAEEAK 1681
                         170       180
                  ....*....|....*....|
gi 392896888  332 MQQRERQKIDVQQAKLEAER 351
Cdd:PTZ00121 1682 KAEEDEKKAAEALKKEAEEA 1701
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
223-349 1.82e-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: 45.71  E-value: 1.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   223 EEERKQFAI-LAKIQAEEKQRRLDEAKEK----LAIDKEKLRLKKEALQRELEERNKAERQKKMD----DEERHREKERQ 293
Cdd:pfam15709  381 EQQRRFEEIrLRKQRLEEERQRQEEEERKqrlqLQAAQERARQQQEEFRRKLQELQRKKQQEEAEraeaEKQRQKELEMQ 460
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392896888   294 KKAERDARLQFAKENaaKLAAQEAKKDISLKSRLEQASMQQRERQKIDV------QQAKLEA 349
Cdd:pfam15709  461 LAEEQKRLMEMAEEE--RLEYQRQKQEAEEKARLEAEERRQKEEEAARLaleeamKQAQEQA 520
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
155-336 1.88e-04

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: 45.94  E-value: 1.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   155 ALESHVREMdhciywiqkyrQAQVRELFEHLanQTADKGKeLRkfLSSILKEIHPPEDYCIKVYDPIGEEERKQFA---- 230
Cdd:pfam01576  689 ALEQQVEEM-----------KTQLEELEDEL--QATEDAK-LR--LEVNMQALKAQFERDLQARDEQGEEKRRQLVkqvr 752
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   231 -ILAKIQAEEKQRRLD-EAKEKLAIDKEKLRLKKEALQRELEERNKAER--QKKMDDEERHREKERqkkAERDARLQFAK 306
Cdd:pfam01576  753 eLEAELEDERKQRAQAvAAKKKLELDLKELEAQIDAANKGREEAVKQLKklQAQMKDLQRELEEAR---ASRDEILAQSK 829
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 392896888   307 ENAAKLAAQEA-----KKDISLKSRLEQASMQQRE 336
Cdd:pfam01576  830 ESEKKLKNLEAellqlQEDLAASERARRQAQQERD 864
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
233-350 1.89e-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: 45.22  E-value: 1.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   233 AKIQAEEKQRRLDEAKEKlaiDKEKLRLKKEALQ-RELEERNKAE--RQKKMDD-----------EERHREKERQKKAER 298
Cdd:TIGR02794   46 GAVAQQANRIQQQKKPAA---KKEQERQKKLEQQaEEAEKQRAAEqaRQKELEQraaaekaakqaEQAAKQAEEKQKQAE 122
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 392896888   299 DARLQFAKENAAKLAAQEAKKdislksRLEQASMQQRERQKIDVQ-QAKLEAE 350
Cdd:TIGR02794  123 EAKAKQAAEAKAKAEAEAERK------AKEEAAKQAEEEAKAKAAaEAKKKAE 169
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
215-357 1.94e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.82  E-value: 1.94e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   215 IKVYDPIGEEERKQFAIlaKIQAE--EKQRRLDEAKEKLAIDKEKLRLkkEALQRELEERNKAERQKkmddEERHREKER 292
Cdd:TIGR02168  189 DRLEDILNELERQLKSL--ERQAEkaERYKELKAELRELELALLVLRL--EELREELEELQEELKEA----EEELEELTA 260
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392896888   293 QKKAER----DARLQFAKENAAKLAAQEAKKDIS-LKSRLEQASMQQRERQKIDVQQAK-LEAERILLLSK 357
Cdd:TIGR02168  261 ELQELEekleELRLEVSELEEEIEELQKELYALAnEISRLEQQKQILRERLANLERQLEeLEAQLEELESK 331
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
225-350 2.02e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.53  E-value: 2.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  225 ERKQFAILAKIQAEEKQRRLDEAKEKLAIDKEKLrlkkEALQRELEERNKAERQKKMDDEERHR------EKERQKKAER 298
Cdd:COG4717   115 REELEKLEKLLQLLPLYQELEALEAELAELPERL----EELEERLEELRELEEELEELEAELAElqeeleELLEQLSLAT 190
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 392896888  299 DARLQFAKENAAKLAAQEAKkdisLKSRLEQAsmqQRERQKIDVQQAKLEAE 350
Cdd:COG4717   191 EEELQDLAEELEELQQRLAE----LEEELEEA---QEELEELEEELEQLENE 235
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
221-351 2.04e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.53  E-value: 2.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  221 IGEEERKQFAILAKIQA-EEKQRRLDEAKEKLA-IDKEKLRLKKEALQRELEERNKAERQKKMDDEERHREKERQKK--A 296
Cdd:COG4717    80 LKEAEEKEEEYAELQEElEELEEELEELEAELEeLREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEelR 159
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392896888  297 ERDARLQFAKENAAKLAAQ--EAKKDIS------LKSRLEQASMQQRERQKIDVQQAKLEAER 351
Cdd:COG4717   160 ELEEELEELEAELAELQEEleELLEQLSlateeeLQDLAEELEELQQRLAELEEELEEAQEEL 222
PTZ00121 PTZ00121
MAEBL; Provisional
223-350 2.13e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.90  E-value: 2.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  223 EEERKqfaILAKIQAEEKQRRLDEAKEKlaidkEKLRLKKEALQRELEERNKAERQKKMDDEERHREKERQKKAERDARL 302
Cdd:PTZ00121 1221 EDAKK---AEAVKKAEEAKKDAEEAKKA-----EEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKA 1292
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 392896888  303 QFAKENAAKLAAQEAKKDISLKSRLEQASMQQRERQKiDVQQAKLEAE 350
Cdd:PTZ00121 1293 DEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKK-KADAAKKKAE 1339
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
236-354 2.35e-04

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: 45.03  E-value: 2.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   236 QAEEKQRRLDEAKEKLAIDKEKLRLKKEALQRELEERNKAERQKKMDD------------EERHREKERQKKAERDarlQ 303
Cdd:pfam15558   66 EKEQRKARLGREERRRADRREKQVIEKESRWREQAEDQENQRQEKLERarqeaeqrkqcqEQRLKEKEEELQALRE---Q 142
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 392896888   304 FAKENAAKLAAQEAKKdiSLKSRLEQASMQQRERQKIDVQQAKL-------EAERILL 354
Cdd:pfam15558  143 NSLQLQERLEEACHKR--QLKEREEQKKVQENNLSELLNHQARKvlvdcqaKAEELLR 198
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
180-347 2.56e-04

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 45.73  E-value: 2.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   180 ELFEHLANQTADKGKELRKFLSSILKEIHPPEDYCIKVYDPIGEEERKQFAILAKIQAEEKQRRLDEAK--EKLAIDKEK 257
Cdd:TIGR00618  176 DQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYltQKREAQEEQ 255
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   258 LRLKKEA--LQRELEE--------------RNKAERQKKMDDEERHREKERQKKAERDARLQ-----FAKENAAKLAAQE 316
Cdd:TIGR00618  256 LKKQQLLkqLRARIEElraqeavleetqerINRARKAAPLAAHIKAVTQIEQQAQRIHTELQskmrsRAKLLMKRAAHVK 335
                          170       180       190
                   ....*....|....*....|....*....|.
gi 392896888   317 AKKDISLKSRLEQASMQQRERQKIDVQQAKL 347
Cdd:TIGR00618  336 QQSSIEEQRRLLQTLHSQEIHIRDAHEVATS 366
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
223-378 2.77e-04

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


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 45.03  E-value: 2.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  223 EEERKQFA-ILAKIQAEEKQRRLDEAKEKLAIDKEKLRLKKEALQRELEERnkAERQKKMDDEERHREKERQKKAERDAR 301
Cdd:COG3064    22 EAEKRAAAeAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELA--AEAAKKLAEAEKAAAEAEKKAAAEKAK 99
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392896888  302 lqfAKENAAKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAERILLLSKYPNFGKGPTAAAATRPQVTAK 378
Cdd:COG3064   100 ---AAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAAR 173
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
238-351 3.07e-04

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: 45.17  E-value: 3.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   238 EEKQRRLDEAKE-KLAIDKEKLRLKKEALqrELEERNKAERQKKMDDEERHR----------------EKERQKKAERDA 300
Cdd:pfam01576  359 EELTEQLEQAKRnKANLEKAKQALESENA--ELQAELRTLQQAKQDSEHKRKklegqlqelqarlsesERQRAELAEKLS 436
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392896888   301 RLQFAKENAAKLAAQEAKKDI-------SLKSRLE--QASMQQRERQKIDV--QQAKLEAER 351
Cdd:pfam01576  437 KLQSELESVSSLLNEAEGKNIklskdvsSLESQLQdtQELLQEETRQKLNLstRLRQLEDER 498
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
234-351 3.37e-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: 44.94  E-value: 3.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   234 KIQAEEKQRRLDEAKEKLAIDKEKLRLKKEALQR--------ELEERNKAE--RQKKMDDEErhrEKERQKKAERDARLQ 303
Cdd:pfam15709  337 RLRAERAEMRRLEVERKRREQEEQRRLQQEQLERaekmreelELEQQRRFEeiRLRKQRLEE---ERQRQEEEERKQRLQ 413
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 392896888   304 FAkenaaklAAQEakkdislKSRLEQASMQ------QRERQKIDVQQAKLEAER 351
Cdd:pfam15709  414 LQ-------AAQE-------RARQQQEEFRrklqelQRKKQQEEAERAEAEKQR 453
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
223-345 4.77e-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: 44.07  E-value: 4.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   223 EEERKQFAILAKiQAEEKQRrldeAKEKLAIDKEKLRLKKealQRELEERNKAERQKKMDDEERHREKERQKK---AERD 299
Cdd:TIGR02794  139 EAERKAKEEAAK-QAEEEAK----AKAAAEAKKKAEEAKK---KAEAEAKAKAEAEAKAKAEEAKAKAEAAKAkaaAEAA 210
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 392896888   300 ARLQFAKENAAKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQA 345
Cdd:TIGR02794  211 AKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAA 256
eIF3_subunit pfam08597
Translation initiation factor eIF3 subunit; This is a family of proteins which are subunits of ...
238-325 5.15e-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: 5.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   238 EEKQRRLDEAKEKlaidKEKLRLKKEALQRELEERNK--AERQKKMDDEERHREKERQKKAERDARLqfakENAAKL--A 313
Cdd:pfam08597   47 KEKAAKAAAAKAK----KKKKSKKQKIAEKEAERKAEeeAEEEEELTPEDEAARKLRLRKAEEESDL----ENAADLfgG 118
                           90
                   ....*....|..
gi 392896888   314 AQEAKKDISLKS 325
Cdd:pfam08597  119 AGDPTKDTDLSS 130
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
174-355 5.35e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.37  E-value: 5.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  174 RQAQVRELFEHLANQTADKGKELRKFlsSILKEIHPPEdycikvydpigeEERKQfailAKIQAEEKQRRLDEAKEKLA- 252
Cdd:COG4717    96 ELEELEEELEELEAELEELREELEKL--EKLLQLLPLY------------QELEA----LEAELAELPERLEELEERLEe 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  253 -----IDKEKLRLKKEALQRELEE---RNKAERQKKMDDEERHREKERQKKAERDARLQFAKENAAKLAAQEAkkdislk 324
Cdd:COG4717   158 lreleEELEELEAELAELQEELEElleQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE------- 230
                         170       180       190
                  ....*....|....*....|....*....|.
gi 392896888  325 sRLEQASMQQRERQKIDVQQAKLEAERILLL 355
Cdd:COG4717   231 -QLENELEAAALEERLKEARLLLLIAAALLA 260
PTZ00121 PTZ00121
MAEBL; Provisional
223-352 5.47e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 5.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  223 EEERKQFAILAKIQAE--EKQRRLDEAKEKlaidKEKLRLKKEAlqRELEERNKAERQKKMDDEER---HREKERQKKAE 297
Cdd:PTZ00121 1094 EEAFGKAEEAKKTETGkaEEARKAEEAKKK----AEDARKAEEA--RKAEDARKAEEARKAEDAKRveiARKAEDARKAE 1167
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  298 RDARLQFAKENAAKLAAQEAKKDISLKS-----RLEQASMQQRERQKIDVQQAKlEAERI 352
Cdd:PTZ00121 1168 EARKAEDAKKAEAARKAEEVRKAEELRKaedarKAEAARKAEEERKAEEARKAE-DAKKA 1226
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
259-342 6.05e-04

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: 43.87  E-value: 6.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   259 RLKKEALQRELeeRNKAERQKkmdDEERHREKERQKKAERDARLQFAKENAAKLAAQEAKkdislKSRLEQASMQQRERQ 338
Cdd:pfam15558   16 RHKEEQRMREL--QQQAALAW---EELRRRDQKRQETLERERRLLLQQSQEQWQAEKEQR-----KARLGREERRRADRR 85

                   ....
gi 392896888   339 KIDV 342
Cdd:pfam15558   86 EKQV 89
Caldesmon pfam02029
Caldesmon;
210-358 6.40e-04

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 44.09  E-value: 6.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   210 PEDYCIKVYDPIGEEERKQFAILAKIQAEEKQRRLDEAKEK-----LAIDKEKLRLKKEALQRELEERNKAERQKKMDDE 284
Cdd:pfam02029   45 EEDSELKPSGQGGLDEEEAFLDRTAKREERRQKRLQEALERqkefdPTIADEKESVAERKENNEEEENSSWEKEEKRDSR 124
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392896888   285 ERHREKERQKKAERDARLQfAKENAAKLAAQEAKKDislksRLEQASMQQRERQKIDVQQAKLEAERILLLSKY 358
Cdd:pfam02029  125 LGRYKEEETEIREKEYQEN-KWSTEVRQAEEEGEEE-----EDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKY 192
TAF4 pfam05236
Transcription initiation factor TFIID component TAF4 family; This region of similarity is ...
226-289 6.51e-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: 6.51e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392896888   226 RKQFAILAKIQAEEKQRRLDEAKEKLA---------IDKEKLRLKKEAlqreleernkAERQKKMDDEERHRE 289
Cdd:pfam05236  113 RKQLKFLAQKDKEEEERRVAEEREGLLkaaksrsnqEDPEQLKLKQEA----------KEMQKEEDEKMRHRA 175
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
223-354 6.88e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 44.28  E-value: 6.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   223 EEERKQFAILAKiQAEEKQRRLDEAKEKLA---IDKEKLRLKKEALQRELEERNKA--ERQKKMDDEERHREKERQKKAE 297
Cdd:TIGR02168  221 ELRELELALLVL-RLEELREELEELQEELKeaeEELEELTAELQELEEKLEELRLEvsELEEEIEELQKELYALANEISR 299
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392896888   298 RDARLQFAKENAAKLAAQEAKKDISL---KSRLE--QASMQQRErQKIDVQQAKLEAERILL 354
Cdd:TIGR02168  300 LEQQKQILRERLANLERQLEELEAQLeelESKLDelAEELAELE-EKLEELKEELESLEAEL 360
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
178-350 8.05e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.90  E-value: 8.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  178 VRELFEHLANQTAdKGKELRKFLSSILKEIHPPEDYcIKVYDPIG------EEERKQFAILAKIQAEEKQRRLDEAKEKL 251
Cdd:PRK03918  326 IEERIKELEEKEE-RLEELKKKLKELEKRLEELEER-HELYEEAKakkeelERLKKRLTGLTPEKLEKELEELEKAKEEI 403
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  252 AIDKEKLRLKKEALQRELEERNKA-ERQKK-----------MDDEERHREKER---------QKKAERDARLQFAKENAA 310
Cdd:PRK03918  404 EEEISKITARIGELKKEIKELKKAiEELKKakgkcpvcgreLTEEHRKELLEEytaelkrieKELKEIEEKERKLRKELR 483
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 392896888  311 KL--AAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAE 350
Cdd:PRK03918  484 ELekVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAE 525
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
222-350 9.10e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.89  E-value: 9.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   222 GEEERKQFAILAKIQAEEKQRRLDEAKEKLAIDKEKLRLKKEALQRELEE-----RNKAER----QKKMDDEERHREKER 292
Cdd:TIGR02168  765 ELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLlneeaANLRERleslERRIAATERRLEDLE 844
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 392896888   293 QKKAERDARLQFAKENAAKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAE 350
Cdd:TIGR02168  845 EQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEE 902
YscO-like pfam16789
YscO-like protein; This family of proteins is similar to the type III secretion protein YscO. ...
240-352 9.91e-04

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: 41.36  E-value: 9.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   240 KQRRLDEAKEKLAIDKEKLRLKKEALQRELEERNKAERQKK---------MDD-----------EERHREKERQKKAERD 299
Cdd:pfam16789   12 KKKRVEEAEKVVKDKKRALEKEKEKLAELEAERDKVRKHKKakmqqlrdeMDRgttsdkilqmkRYIKVVKERLKQEEKK 91
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 392896888   300 ARLQFAKENAAKLAAQEAKKDISLKSRLEQASMQQRERQkidVQQAKLEAERI 352
Cdd:pfam16789   92 VQDQKEQVRTAARNLEIAREELKKKRQEVEKLEKHKKEW---VKEMKKEEEDQ 141
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
247-301 1.09e-03

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


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 43.60  E-value: 1.09e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 392896888   247 AKEKLAIDKEKL--RLKKEALQRELEERNKaERQKkmdDEERHREKERQKKAERDAR 301
Cdd:pfam03154  581 AGSKLAKKREEAleKAKREAEQKAREEKER-EKEK---EKEREREREREREAERAAK 633
PRK12705 PRK12705
hypothetical protein; Provisional
223-351 1.26e-03

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 43.16  E-value: 1.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  223 EEERKQFAILAKIQAEEKQRRLDEAKEKLAIDKEKLRLKKEALQRELEERNKAERQKkmDDEERHREKERQKKAERDARL 302
Cdd:PRK12705   51 EAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQL--EEREKALSARELELEELEKQL 128
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 392896888  303 QFAKENAAKLAAQEAKKDI--SLKSRLEQasmQQRERQKIDVQQAKLEAER 351
Cdd:PRK12705  129 DNELYRVAGLTPEQARKLLlkLLDAELEE---EKAQRVKKIEEEADLEAER 176
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
221-316 1.27e-03

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 43.19  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  221 IGEEERKQFAILAKIQAEEKQRRLdEAKEKLAIDKEKL-RLKKEALQRELEERNKAERQKKMDDEERHREKERQKKAERD 299
Cdd:PTZ00266  440 IEKENAHRKALEMKILEKKRIERL-EREERERLERERMeRIERERLERERLERERLERDRLERDRLDRLERERVDRLERD 518
                          90
                  ....*....|....*..
gi 392896888  300 aRLQFAKENAAKLAAQE 316
Cdd:PTZ00266  519 -RLEKARRNSYFLKGME 534
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
180-351 1.37e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 1.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  180 ELFEHLANQTADKGKELRKFLSSILKEIHPPEDycikVYDPIGEEERKQFAILAKIQaeEKQRRLDEAKEKLA-IDKEKL 258
Cdd:PRK03918  158 DDYENAYKNLGEVIKEIKRRIERLEKFIKRTEN----IEELIKEKEKELEEVLREIN--EISSELPELREELEkLEKEVK 231
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  259 RLKK-----EALQRELEERNKaerqKKMDDEERHREKERQKKaERDARLQFAKENAAKLaaQEAKKDISLKSRLEQASMQ 333
Cdd:PRK03918  232 ELEElkeeiEELEKELESLEG----SKRKLEEKIRELEERIE-ELKKEIEELEEKVKEL--KELKEKAEEYIKLSEFYEE 304
                         170
                  ....*....|....*....
gi 392896888  334 QRER-QKIDVQQAKLEAER 351
Cdd:PRK03918  305 YLDElREIEKRLSRLEEEI 323
CCDC47 pfam07946
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ...
223-298 1.40e-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: 42.55  E-value: 1.40e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392896888   223 EEERKQFAilaKIQAEEKQrrldeakEKLAIDKEKLRLKKEalqRELEERNKAERQKKMDdeerhrEKERQKKAER 298
Cdd:pfam07946  267 EEEIEKIK---KAAEEERA-------EEAQEKKEEAKKKER---EEKLAKLSPEEQRKYE------EKERKKEQRK 323
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
223-352 1.53e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.58  E-value: 1.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  223 EEERKQfailAKIQAEEKQRRLDEAKEKLAIDKEKLRLKKEALQRELEERNKAERQKKmddeerHREKERQKKAERDARL 302
Cdd:COG4372    65 EEELEQ----ARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELE------ELQKERQDLEQQRKQL 134
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 392896888  303 QfakENAAKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAERI 352
Cdd:COG4372   135 E---AQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEA 181
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
234-354 1.58e-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: 1.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   234 KIQAEEKQRRLDEAKEKLA----IDKEkLRLKKEALQRELEernKAERQKKMDDEERHREKE------RQKKAERDARLQ 303
Cdd:TIGR02168  171 KERRKETERKLERTRENLDrledILNE-LERQLKSLERQAE---KAERYKELKAELRELELAllvlrlEELREELEELQE 246
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 392896888   304 FAKENA---AKLAAQEAKKDISL-KSRLEQASMQqrerQKIDVQQAKLEAERILL 354
Cdd:TIGR02168  247 ELKEAEeelEELTAELQELEEKLeELRLEVSELE----EEIEELQKELYALANEI 297
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
247-357 1.61e-03

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


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 42.72  E-value: 1.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  247 AKEKLAIDKEKLRLKKEALQRELEERNKAERQKKMDDE---ERHREKERQKKAERDARLQFA--KENAAKLAAQEAKKdi 321
Cdd:COG3064     1 AQEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEaeeERLAELEAKRQAEEEAREAKAeaEQRAAELAAEAAKK-- 78
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 392896888  322 slKSRLEQASMQQRERQKIDVQQAKLEAERILLLSK 357
Cdd:COG3064    79 --LAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEK 112
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
223-351 1.66e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 1.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  223 EEERKQFAILAKIQAEEKQRRLDEAKEKLAIDKEKLRLKKEALQRELEERNK--------------AERQKKMDDEERHR 288
Cdd:COG4717   369 EQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEEllealdeeeleeelEELEEELEELEEEL 448
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392896888  289 EKERQKKAERDARLQFAkENAAKLAAQEAKKDiSLKSRLEQASmqqRERQKIDVQQAKLEAER 351
Cdd:COG4717   449 EELREELAELEAELEQL-EEDGELAELLQELE-ELKAELRELA---EEWAALKLALELLEEAR 506
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
225-336 1.72e-03

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 42.89  E-value: 1.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   225 ERKQFAILAKI-----QAEEKQRRLDEAKEKLA--------------------IDKEKL--RLKKealQRELEERNKAER 277
Cdd:pfam10174  393 ERKINVLQKKIenlqeQLRDKDKQLAGLKERVKslqtdssntdtalttleealSEKERIieRLKE---QREREDRERLEE 469
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392896888   278 QKKMDDEERHREKE----RQKKAERDARLQFAKENAAKLAAQEAKKDISLKSrLEQASMQQRE 336
Cdd:pfam10174  470 LESLKKENKDLKEKvsalQPELTEKESSLIDLKEHASSLASSGLKKDSKLKS-LEIAVEQKKE 531
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
170-351 1.90e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 42.75  E-value: 1.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   170 IQKYRQAQVRELFEHLANQTADKGKELRKfLSSILKEIhppEDYCIKVyDPIGEE--ERKQFAILAKIQAEEKQRRLDEA 247
Cdd:TIGR02169  309 SIAEKERELEDAEERLAKLEAEIDKLLAE-IEELEREI---EEERKRR-DKLTEEyaELKEELEDLRAELEEVDKEFAET 383
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   248 KEKLAidkeKLRLKKEALQRELEE------RNKAERQKKMDDEERHREK---ERQKKAERDARLqfaKENAAKLAAQEAK 318
Cdd:TIGR02169  384 RDELK----DYREKLEKLKREINElkreldRLQEELQRLSEELADLNAAiagIEAKINELEEEK---EDKALEIKKQEWK 456
                          170       180       190
                   ....*....|....*....|....*....|...
gi 392896888   319 kdisLKSRLEQASMQQRERQKIDVQQAKLEAER 351
Cdd:TIGR02169  457 ----LEQLAADLSKYEQELYDLKEEYDRVEKEL 485
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
239-350 2.17e-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: 42.74  E-value: 2.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   239 EKQRRLDEAKEKLAIDKEKLRLKKEAL------QRELEERNKAERQKKMDDEERHR---------EKERQKKAERDARLQ 303
Cdd:TIGR02168  674 ERRREIEELEEKIEELEEKIAELEKALaelrkeLEELEEELEQLRKELEELSRQISalrkdlarlEAEVEQLEERIAQLS 753
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 392896888   304 FAKENAAKLAAQEAKKDISLKSRLEQASmQQRERQKIDVQQAKLEAE 350
Cdd:TIGR02168  754 KELTELEAEIEELEERLEEAEEELAEAE-AEIEELEAQIEQLKEELK 799
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
221-322 2.27e-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: 2.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  221 IGEEERKQFAILAKIQAE--EKQRRLDEAKEKLAIDKEKLRLKKEALQRELEERNKAerQKKMDDEERHREKERQKKAER 298
Cdd:COG4942   144 LAPARREQAEELRADLAElaALRAELEAERAELEALLAELEEERAALEALKAERQKL--LARLEKELAELAAELAELQQE 221
                          90       100
                  ....*....|....*....|....
gi 392896888  299 DARLQFAKENAAKLAAQEAKKDIS 322
Cdd:COG4942   222 AEELEALIARLEAEAAAAAERTPA 245
cdk7 TIGR00570
CDK-activating kinase assembly factor MAT1; All proteins in this family for which functions ...
174-329 2.46e-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: 41.71  E-value: 2.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   174 RQAQVR-ELFEhlaNQTADKGKELRKflsSILKEIHPPED--YCIKVYDPIGEE-ERKQFAILAKIQAEEKQRRLD---- 245
Cdd:TIGR00570   54 RKNNFRvQLFE---DPTVEKEVDIRK---RVLKIYNKREEdfPSLREYNDYLEEvEDIVYNLTNNIDLENTKKKIEtyqk 127
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   246 EAKEKLAIDKEKLRLKKEALQRELEERNKAERQKKMDDEERHREKERQKKAERDA---RLQFAKENAAKLAAQEAKKDIS 322
Cdd:TIGR00570  128 ENKDVIQKNKEKSTREQEELEEALEFEKEEEEQRRLLLQKEEEEQQMNKRKNKQAlldELETSTLPAAELIAQHKKNSVK 207

                   ....*..
gi 392896888   323 LKSRLEQ 329
Cdd:TIGR00570  208 LEMQVEK 214
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
177-316 2.49e-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: 2.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   177 QVRELFEHLANQTADKgkELRKFLSSILKEIHPPEDYCIKVYDPIGEEERKQFAILAKIQAEEKQRRLDEAKEKLAIDKE 256
Cdd:TIGR00618  373 QQHTLTQHIHTLQQQK--TTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCT 450
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392896888   257 KLRLK-KEALQRELEERNKAERQKKMDDEERHrEKERQKKAERDARLQFAKENAAKLAAQE 316
Cdd:TIGR00618  451 AQCEKlEKIHLQESAQSLKEREQQLQTKEQIH-LQETRKKAVVLARLLELQEEPCPLCGSC 510
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
217-353 2.57e-03

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


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 39.34  E-value: 2.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  217 VYDPIGE--EERKQfailaKIQAEekqrrLDEAKEKlaidKEKLRLKKEALQRELEERnKAERQKKMDDEERHREKERQK 294
Cdd:cd06503    20 LWKPILKalDEREE-----KIAES-----LEEAEKA----KEEAEELLAEYEEKLAEA-RAEAQEIIEEARKEAEKIKEE 84
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 392896888  295 KAERdarlqfAKENAAKLAAQeAKKDIslksRLEQASMQQRERQKIdVQQAKLEAERIL 353
Cdd:cd06503    85 ILAE------AKEEAERILEQ-AKAEI----EQEKEKALAELRKEV-ADLAVEAAEKIL 131
PRK05035 PRK05035
electron transport complex protein RnfC; Provisional
233-350 2.71e-03

electron transport complex protein RnfC; Provisional


Pssm-ID: 235334 [Multi-domain]  Cd Length: 695  Bit Score: 42.24  E-value: 2.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  233 AKIQA-EEKQRRLDEAKEKLAidkeklrLKKEALQREleernKAERqkkmddEERHREKERQKKAERDARLQFAKE--NA 309
Cdd:PRK05035  436 AEIRAiEQEKKKAEEAKARFE-------ARQARLERE-----KAAR------EARHKKAAEARAAKDKDAVAAALArvKA 497
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 392896888  310 AKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAE 350
Cdd:PRK05035  498 KKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQ 538
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
233-357 2.96e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.43  E-value: 2.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  233 AKIQAEEKQRRLDEAKEKLaidkEKLRLKKEALQRELEERNKaERQKKmddeerhrekeRQKKAERDARLQFAKENAAKL 312
Cdd:COG4372    36 ALFELDKLQEELEQLREEL----EQAREELEQLEEELEQARS-ELEQL-----------EEELEELNEQLQAAQAELAQA 99
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 392896888  313 AAQeakkdisLKSRLEQASMQQRERQKIDVQQAKLEAERILLLSK 357
Cdd:COG4372   100 QEE-------LESLQEEAEELQEELEELQKERQDLEQQRKQLEAQ 137
Taxilin pfam09728
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ...
226-358 2.96e-03

Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.


Pssm-ID: 462861 [Multi-domain]  Cd Length: 302  Bit Score: 41.09  E-value: 2.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   226 RKQFAILakiQAEEKQRRLDEAKEKLAidKEKLrlkkEALQRELEERNKA---ERQKKMDDEERHR----EKERQKKAER 298
Cdd:pfam09728   45 KKKQDQL---QKEKDQLQSELSKAILA--KSKL----EKLCRELQKQNKKlkeESKKLAKEEEEKRkelsEKFQSTLKDI 115
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392896888   299 DARLQFAKENAAKLAAQE---AKKdisLKSRLEQasMQQRErQKIDVQQAKLEAERILLLSKY 358
Cdd:pfam09728  116 QDKMEEKSEKNNKLREENeelREK---LKSLIEQ--YELRE-LHFEKLLKTKELEVQLAEAKL 172
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
222-351 2.96e-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: 42.08  E-value: 2.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   222 GEEERKQFAI---LAKIQAEEKQrrldEAKEKLaiDKEKLRLKKE------ALQRELEERNKAE-RQKKMDD---EERH- 287
Cdd:pfam01576  543 LEEGKKRLQReleALTQQLEEKA----AAYDKL--EKTKNRLQQElddllvDLDHQRQLVSNLEkKQKKFDQmlaEEKAi 616
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392896888   288 --REKERQKKAERDARLQFAKenAAKLA-----AQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAER 351
Cdd:pfam01576  617 saRYAEERDRAEAEAREKETR--ALSLAraleeALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELER 685
Caldesmon pfam02029
Caldesmon;
223-301 3.12e-03

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 41.78  E-value: 3.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   223 EEERKQFaILAKIQAEEKQRRLDEAKEKlaiDKEKLRLKKEALQRELEERNKA--ERQKKMDDEERHR---EKERQKKAE 297
Cdd:pfam02029  237 EEEAEVF-LEAEQKLEELRRRRQEKESE---EFEKLRQKQQEAELELEELKKKreERRKLLEEEEQRRkqeEAERKLREE 312

                   ....
gi 392896888   298 RDAR 301
Cdd:pfam02029  313 EEKR 316
NPIP pfam06409
Nuclear pore complex interacting protein (NPIP); This family consists of a series of primate ...
225-302 3.54e-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: 3.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   225 ERKQFAILAKIQAEEKQRRLDEAKEKLAIDKEKLRlKKEALQRELEERNK----AERQKKMDDEERHREKERQKKAERDA 300
Cdd:pfam06409   93 ERKQEAIICKLEDIFKLNRHDEIKGKAKIAKEHLR-KKSMKEDEHGEKEKqakeAEEKGKLDEKEHGEKEEMFQEAEALG 171

                   ..
gi 392896888   301 RL 302
Cdd:pfam06409  172 KL 173
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
175-351 3.55e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.82  E-value: 3.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  175 QAQVRELFEHL--ANQTADKGKELRKFLSSILKEIHPPEDYcikvydpiGEEERKQFAILAKIQA-EEKQRRLDEAKEKL 251
Cdd:COG4913   616 EAELAELEEELaeAEERLEALEAELDALQERREALQRLAEY--------SWDEIDVASAEREIAElEAELERLDASSDDL 687
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  252 aidkEKLRLKKEALQRELEErNKAERQKKMDDEERHREKERQKKAERDaRLQFAKENAAKLAAQEAKKDisLKSRLEQAS 331
Cdd:COG4913   688 ----AALEEQLEELEAELEE-LEEELDELKGEIGRLEKELEQAEEELD-ELQDRLEAAEDLARLELRAL--LEERFAAAL 759
                         170       180
                  ....*....|....*....|...
gi 392896888  332 MQQRE---RQKIDVQQAKLEAER 351
Cdd:COG4913   760 GDAVErelRENLEERIDALRARL 782
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
222-345 3.67e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.56  E-value: 3.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  222 GEEERKQfAILAKIQAEEKQRRLDEAKEKLAIDKEKL-RLKK--------EALQRELEERN-KAERQKKMDDEERHREKE 291
Cdd:PRK02224  553 AEEKREA-AAEAEEEAEEAREEVAELNSKLAELKERIeSLERirtllaaiADAEDEIERLReKREALAELNDERRERLAE 631
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 392896888  292 RQkkaERDARLQFAKENAAKLAAQEAKKdiSLKSRLEQAS--MQQRERQKIDVQQA 345
Cdd:PRK02224  632 KR---ERKRELEAEFDEARIEEAREDKE--RAEEYLEQVEekLDELREERDDLQAE 682
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
223-361 3.68e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.43  E-value: 3.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  223 EEERKQFAILAKIQAEekQRRLDEAKEKLAIDKEKLRLKKEALQRELEERNKAERQKKMDDEERHREKERQKKAERDARL 302
Cdd:COG4372   108 EEAEELQEELEELQKE--RQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQAL 185
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 392896888  303 QFAKENAAKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAERILLLSKYPNF 361
Cdd:COG4372   186 DELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALEL 244
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
181-379 4.01e-03

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


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 41.75  E-value: 4.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   181 LFEHLANQTADKGKELRKFLSSIL---KEIHPpedyciKVYDPIGEEERKQFAI---LAKIQA-------EEKQRRLDEA 247
Cdd:pfam12128  536 LLHFLRKEAPDWEQSIGKVISPELlhrTDLDP------EVWDGSVGGELNLYGVkldLKRIDVpewaaseEELRERLDKA 609
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   248 KEKL--------AIDKE--KLRLKKEALQRELEE-----RNKAERQKKMDDEerHREKERQKKAERDARLQFAKENAAKL 312
Cdd:pfam12128  610 EEALqsarekqaAAEEQlvQANGELEKASREETFartalKNARLDLRRLFDE--KQSEKDKKNKALAERKDSANERLNSL 687
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392896888   313 AAQeaKKDISLKsrlEQASMQQRERQKIDVQQAKLEAERILLLSKYPNFGKGPTAAAATRPQVTAKQ 379
Cdd:pfam12128  688 EAQ--LKQLDKK---HQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAEL 749
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
171-349 4.25e-03

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 41.42  E-value: 4.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   171 QKYRQAQVRELFEHLANQTADKGKELRKFLSSiLKEIHPPEDYCIKVYDPIGEEERKQFAILAKiQAEEKQRRLDEAKEK 250
Cdd:pfam07888   60 EKERYKRDREQWERQRRELESRVAELKEELRQ-SREKHEELEEKYKELSASSEELSEEKDALLA-QRAAHEARIRELEED 137
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   251 LAIDKEKLRLKKEALQRELEERNKAERQKKMDDEER---------------HREKERQK----KAERDARLQFAKENAAK 311
Cdd:pfam07888  138 IKTLTQRVLERETELERMKERAKKAGAQRKEEEAERkqlqaklqqteeelrSLSKEFQElrnsLAQRDTQVLQLQDTITT 217
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392896888   312 L-----------AAQEA-KKDI-SLKSRL------------EQASM-QQRERQKIDVQQAKLEA 349
Cdd:pfam07888  218 LtqklttahrkeAENEAlLEELrSLQERLnaserkveglgeELSSMaAQRDRTQAELHQARLQA 281
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
266-352 4.35e-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: 4.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   266 QRELEERNKAERQKKMDDEERHREKErQKKAERDARLQFAKENAAKLAAQEakKDISLKSRLEQASMQ-QRERQKIDVQQ 344
Cdd:pfam17380  281 QKAVSERQQQEKFEKMEQERLRQEKE-EKAREVERRRKLEEAEKARQAEMD--RQAAIYAEQERMAMErERELERIRQEE 357

                   ....*...
gi 392896888   345 AKLEAERI 352
Cdd:pfam17380  358 RKRELERI 365
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
263-354 5.36e-03

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 41.09  E-value: 5.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  263 EALQRELEeRNKAERQKKMDDEERHREKERQKKAERDARLQFAKENAAKLAAQEAKKDiSLKSRLEQASMQQRERQKIDV 342
Cdd:PRK11448  145 HALQQEVL-TLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLE-QLQEKAAETSQERKQKRKEIT 222
                          90
                  ....*....|..
gi 392896888  343 QQAkleAERILL 354
Cdd:PRK11448  223 DQA---AKRLEL 231
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
263-351 7.07e-03

Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.


Pssm-ID: 464003 [Multi-domain]  Cd Length: 119  Bit Score: 37.93  E-value: 7.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   263 EALQRELEERnKAERQKKMDDEERHREKERQKKAERDARLQ----FAKENAAKL--AAQEAKKDISLKSRLEQasmqqrE 336
Cdd:pfam13863    9 FLVQLALDAK-REEIERLEELLKQREEELEKKEQELKEDLIkfdkFLKENDAKRrrALKKAEEETKLKKEKEK------E 81
                           90
                   ....*....|....*
gi 392896888   337 RQKIDVQQAKLEAER 351
Cdd:pfam13863   82 IKKLTAQIEELKSEI 96
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
253-351 7.15e-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: 40.21  E-value: 7.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   253 IDKEKLRLKKEALQRELEERNKAERQKKMDDEERHREKERQKKAE----RDARLQFAKENAAKLAAQEAKKDISLKSRLE 328
Cdd:TIGR02794   43 VDPGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEqarqKELEQRAAAEKAAKQAEQAAKQAEEKQKQAE 122
                           90       100
                   ....*....|....*....|...
gi 392896888   329 QASMQQRERQKidvqqAKLEAER 351
Cdd:TIGR02794  123 EAKAKQAAEAK-----AKAEAEA 140
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
232-302 7.27e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.52  E-value: 7.27e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392896888  232 LAKIQAEEKQRRLDEAKEKLAIDKEKLRLKKEALQRELEERnKAERQKKM---DDEERHREKERQKKAER-DARL 302
Cdd:COG1579   103 RRISDLEDEILELMERIEELEEELAELEAELAELEAELEEK-KAELDEELaelEAELEELEAEREELAAKiPPEL 176
PRK01294 PRK01294
lipase secretion chaperone;
222-351 7.45e-03

lipase secretion chaperone;


Pssm-ID: 234937 [Multi-domain]  Cd Length: 336  Bit Score: 40.05  E-value: 7.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888  222 GEEERKQFAILAKIQ--------AEEKQRRLDEAKEKLAIDkEKLRLKKEALQRELEERNKAERQKKMDDEERhrekerq 293
Cdd:PRK01294  182 GEENQYQRYALERLRiaqdpslsDAQKAARLAALEAQLPED-LRAALQESQRQQALLQQLAQLQASGASPQEL------- 253
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 392896888  294 kkaeRDARLQFAKENAAKLAAQEAKKDISLKSRLEQasmQQRERQKIDVQQAKLEAER 351
Cdd:PRK01294  254 ----RLMRAQLVGPEAAQRLEQLDQQRAAWQQRYDD---YLAQRAQILNAAGLSPQDR 304
CCDC34 pfam13904
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ...
223-311 7.46e-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: 39.30  E-value: 7.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   223 EEERKQfaiLAKIQAEE--KQRRLDEAKEKLAIDKEKLRLK---------KEALQRELEERNKAERQKKMDDEERHREKE 291
Cdd:pfam13904   86 AELRKR---LAKEKYQEwlQRKARQQTKKREESHKQKAAESaskslakpeRKVSQEEAKEVLQEWERKKLEQQQRKREEE 162
                           90       100
                   ....*....|....*....|
gi 392896888   292 RQKKAERDARLQFAKENAAK 311
Cdd:pfam13904  163 QREQLKKEEEEQERKQLAEK 182
UDM1_RNF168_RNF169-like cd22249
UDM1 (ubiquitin-dependent DSB recruitment module 1) found in RING finger proteins RNF168, ...
255-302 9.03e-03

UDM1 (ubiquitin-dependent DSB recruitment module 1) found in RING finger proteins RNF168, RNF169 and similar proteins; This model represents the UDM1 (ubiquitin-dependent double-strand break [DSB] recruitment module 1) found in RING finger proteins, RNF168 and RNF169. RNF168 is an E3 ubiquitin-protein ligase that promotes non-canonical K27 ubiquitination to signal DNA damage. It functions, together with RNF8, as a DNA damage response (DDR) factor that promotes a series of ubiquitylation events on substrates such as H2A and H2AX. With H2AK13/15 ubiquitylation, it facilitates recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of double-strand breaks (DSBs), and inhibits homologous recombination (HR) in cells deficient in the tumor suppressor BRCA1. RNF168 also promotes H2A neddylation, which antagonizes ubiquitylation of H2A and regulates DNA damage repair. In addition, RNF168 forms a functional complex with RAD6A or RAD6B during the DNA damage response. RNF169 is an uncharacterized E3 ubiquitin-protein ligase paralogous to RNF168. It functions as a negative regulator of the DNA damage signaling cascade. RNF169 recognizes polyubiquitin structures but does not itself contribute to double-strand break (DSB)-induced chromatin ubiquitylation. It contributes to the regulation of DSB repair pathway utilization via functionally competing with recruiting repair factors, 53BP1 and RAP80-BRCA1, for association with RNF168-modified chromatin, independent of its catalytic activity, limiting the magnitude of the RNF8/RNF168-dependent signaling response to DSBs. The UDM1 domain comprises LRM1 (LR motif 1), UMI (ubiquitin-interacting motif [UIM]- and MIU-related UBD) and MIU1 (motif interacting with ubiquitin 1). Mutations of Ub-interacting residues in UDM1 have little effect on the accumulation of RNF168 to DSB sites, suggesting that it may not be the main site of binding ubiquitylated and polyubiquitylated targets.


Pssm-ID: 409016 [Multi-domain]  Cd Length: 66  Bit Score: 36.09  E-value: 9.03e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 392896888  255 KEKLRLKKEALQRELEERNKAER--QKKMDDEERHREKERQKKAERDARL 302
Cdd:cd22249    13 AQLKKLEEERRKEREEEEKASEEliRKLQEEEERQRKREREEQLKQDEEL 62
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
238-356 9.98e-03

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: 38.89  E-value: 9.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896888   238 EEKQRRLDEAKEKLAidkeklrlKKEALQRELEERNKAERQkkmddeerhREKERQKKAErdARLQFAKENAAKLAAQEA 317
Cdd:pfam04012   32 RDMQSELVKARQALA--------QTIARQKQLERRLEQQTE---------QAKKLEEKAQ--AALTKGNEELAREALAEK 92
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 392896888   318 KKDISLKSRLEQASMQQRER--------QKIDVQQAKLEAERILLLS 356
Cdd:pfam04012   93 KSLEKQAEALETQLAQQRSAveqlrkqlAALETKIQQLKAKKNLLKA 139
 
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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