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Conserved domains on  [gi|392896884|ref|NP_001255156|]
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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
805-986 3.92e-11

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 68.63  E-value: 3.92e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  805 IQKYRQAQVRELFEHLANQTAD---KGKELRKFLSSILKEihppedycikvydpigEEERKQFAILAKIQAEEKQR--RL 879
Cdd:PTZ00121 1589 AEEARIEEVMKLYEEEKKMKAEeakKAEEAKIKAEELKKA----------------EEEKKKVEQLKKKEAEEKKKaeEL 1652
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  880 DEAKEKLAIDKEKLRLKKEALQRELEERNKAERQKKMDDEERHREKERQKKAE----------RDARLQFAKENAAKLAA 949
Cdd:PTZ00121 1653 KKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEelkkkeaeekKKAEELKKAEEENKIKA 1732
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 392896884  950 QEAKKDISL-KSRLEQASMQQRERQKIdvQQAKLEAER 986
Cdd:PTZ00121 1733 EEAKKEAEEdKKKAEEAKKDEEEKKKI--AHLKKEEEK 1768
 
Name Accession Description Interval E-value
PTZ00121 PTZ00121
MAEBL; Provisional
805-986 3.92e-11

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 68.63  E-value: 3.92e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  805 IQKYRQAQVRELFEHLANQTAD---KGKELRKFLSSILKEihppedycikvydpigEEERKQFAILAKIQAEEKQR--RL 879
Cdd:PTZ00121 1589 AEEARIEEVMKLYEEEKKMKAEeakKAEEAKIKAEELKKA----------------EEEKKKVEQLKKKEAEEKKKaeEL 1652
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  880 DEAKEKLAIDKEKLRLKKEALQRELEERNKAERQKKMDDEERHREKERQKKAE----------RDARLQFAKENAAKLAA 949
Cdd:PTZ00121 1653 KKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEelkkkeaeekKKAEELKKAEEENKIKA 1732
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 392896884  950 QEAKKDISL-KSRLEQASMQQRERQKIdvQQAKLEAER 986
Cdd:PTZ00121 1733 EEAKKEAEEdKKKAEEAKKDEEEKKKI--AHLKKEEEK 1768
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
858-973 6.40e-11

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: 62.37  E-value: 6.40e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   858 EEERKQfailAKIQA--EEKQRRLDEAKEKLAIDKEKLRLKKEALQRELEERNKAERQKKMDDE-----ERHREKERQKK 930
Cdd:pfam05672   17 AEKRRQ----AREQRerEEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEErqrkaEEEAEEREQRE 92
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 392896884   931 AERDARLQFAKENAAKLAAQEAKkdislKSRLEQASMQQRERQ 973
Cdd:pfam05672   93 QEEQERLQKQKEEAEAKAREEAE-----RQRQEREKIMQQEEQ 130
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
858-986 3.29e-10

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: 64.10  E-value: 3.29e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   858 EEERKQFAILAKIQAEEKQRRLDEAKEKLAidKEKLRLKKEALQRELEERNK----AERQKKMDDEERHREKERQKKAER 933
Cdd:TIGR02794  108 EQAAKQAEEKQKQAEEAKAKQAAEAKAKAE--AEAERKAKEEAAKQAEEEAKakaaAEAKKKAEEAKKKAEAEAKAKAEA 185
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 392896884   934 DARlqfAKENAAKLAAQEAKKdislKSRLEQASMQQRERQKidvqQAKLEAER 986
Cdd:TIGR02794  186 EAK---AKAEEAKAKAEAAKA----KAAAEAAAKAEAEAAA----AAAAEAER 227
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
809-992 3.62e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 65.34  E-value: 3.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  809 RQAQVRELFEHLANQTADKGKELRKFLSSILKEIHppedycikvyDPIGEEERKQFAILAKIQAEEKQRRLDEAKEKLAI 888
Cdd:COG1196   268 ELEELRLELEELELELEEAQAEEYELLAELARLEQ----------DIARLEERRRELEERLEELEEELAELEEELEELEE 337
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  889 DKEKLRLKKEALQRELEERNKAERQKK---MDDEERHREKERQKKAERDARLQFAKEnAAKLAAQEAKKDISLKSRLEQA 965
Cdd:COG1196   338 ELEELEEELEEAEEELEEAEAELAEAEealLEAEAELAEAEEELEELAEELLEALRA-AAELAAQLEELEEAEEALLERL 416
                         170       180
                  ....*....|....*....|....*..
gi 392896884  966 SMQQRERQKIDVQQAKLEAERILLLSK 992
Cdd:COG1196   417 ERLEEELEELEEALAELEEEEEEEEEA 443
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
857-984 1.04e-04

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


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 46.42  E-value: 1.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  857 GEEERKQFaiLAKIQAEEKQ-RRLDEAKEKLAIDKEKLRLKKEAL---QRELEERNKAERQKKMDDEERHREKERQ--KK 930
Cdd:cd16269   168 AEEVLQEF--LQSKEAEAEAiLQADQALTEKEKEIEAERAKAEAAeqeRKLLEEQQRELEQKLEDQERSYEEHLRQlkEK 245
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 392896884  931 AERDARLQfakenaaklaAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEA 984
Cdd:cd16269   246 MEEERENL----------LKEQERALESKLKEQEALLEEGFKEQAELLQEEIRS 289
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
865-977 9.73e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 38.33  E-value: 9.73e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884    865 AILAKIQAEEKQRRlDEAKEKlaidKEKLRLKKEALQRELEERNKAERQKKmddeerhrEKERQKKAERDARLQFAKENA 944
Cdd:smart00935   18 AAQKQLEKEFKKRQ-AELEKL----EKELQKLKEKLQKDAATLSEAAREKK--------EKELQKKVQEFQRKQQKLQQD 84
                            90       100       110
                    ....*....|....*....|....*....|...
gi 392896884    945 AKLAAQEAKKDISlkSRLEQASMQQRERQKIDV 977
Cdd:smart00935   85 LQKRQQEELQKIL--DKINKAIKEVAKKKGYDL 115
 
Name Accession Description Interval E-value
PTZ00121 PTZ00121
MAEBL; Provisional
805-986 3.92e-11

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 68.63  E-value: 3.92e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  805 IQKYRQAQVRELFEHLANQTAD---KGKELRKFLSSILKEihppedycikvydpigEEERKQFAILAKIQAEEKQR--RL 879
Cdd:PTZ00121 1589 AEEARIEEVMKLYEEEKKMKAEeakKAEEAKIKAEELKKA----------------EEEKKKVEQLKKKEAEEKKKaeEL 1652
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  880 DEAKEKLAIDKEKLRLKKEALQRELEERNKAERQKKMDDEERHREKERQKKAE----------RDARLQFAKENAAKLAA 949
Cdd:PTZ00121 1653 KKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEelkkkeaeekKKAEELKKAEEENKIKA 1732
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 392896884  950 QEAKKDISL-KSRLEQASMQQRERQKIdvQQAKLEAER 986
Cdd:PTZ00121 1733 EEAKKEAEEdKKKAEEAKKDEEEKKKI--AHLKKEEEK 1768
PTZ00121 PTZ00121
MAEBL; Provisional
859-986 4.67e-11

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 68.63  E-value: 4.67e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  859 EERKQFAILAKIQAEEKQRRLDEAKEKLAIDKEKL---RLKKEALQRELEERNKAERQKKMDDEERHREKERQKKAERDA 935
Cdd:PTZ00121 1339 EEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKeeaKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKK 1418
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 392896884  936 RLQFAKENA-AKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAER 986
Cdd:PTZ00121 1419 KADEAKKKAeEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAK 1470
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
858-973 6.40e-11

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: 62.37  E-value: 6.40e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   858 EEERKQfailAKIQA--EEKQRRLDEAKEKLAIDKEKLRLKKEALQRELEERNKAERQKKMDDE-----ERHREKERQKK 930
Cdd:pfam05672   17 AEKRRQ----AREQRerEEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEErqrkaEEEAEEREQRE 92
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 392896884   931 AERDARLQFAKENAAKLAAQEAKkdislKSRLEQASMQQRERQ 973
Cdd:pfam05672   93 QEEQERLQKQKEEAEAKAREEAE-----RQRQEREKIMQQEEQ 130
PTZ00121 PTZ00121
MAEBL; Provisional
854-986 2.43e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 66.32  E-value: 2.43e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  854 DPIGEEERKQFAILAKIQAEEKqRRLDEAKEKLAIDKEK---LRLKKEALQRELEERNKAERQKKMDD-----EERHREK 925
Cdd:PTZ00121 1369 AEKKKEEAKKKADAAKKKAEEK-KKADEAKKKAEEDKKKadeLKKAAAAKKKADEAKKKAEEKKKADEakkkaEEAKKAD 1447
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392896884  926 ERQKKAERDARLQFAKENA--------AKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAER 986
Cdd:PTZ00121 1448 EAKKKAEEAKKAEEAKKKAeeakkadeAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAK 1516
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
858-986 3.29e-10

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: 64.10  E-value: 3.29e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   858 EEERKQFAILAKIQAEEKQRRLDEAKEKLAidKEKLRLKKEALQRELEERNK----AERQKKMDDEERHREKERQKKAER 933
Cdd:TIGR02794  108 EQAAKQAEEKQKQAEEAKAKQAAEAKAKAE--AEAERKAKEEAAKQAEEEAKakaaAEAKKKAEEAKKKAEAEAKAKAEA 185
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 392896884   934 DARlqfAKENAAKLAAQEAKKdislKSRLEQASMQQRERQKidvqQAKLEAER 986
Cdd:TIGR02794  186 EAK---AKAEEAKAKAEAAKA----KAAAEAAAKAEAEAAA----AAAAEAER 227
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
809-992 3.62e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 65.34  E-value: 3.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  809 RQAQVRELFEHLANQTADKGKELRKFLSSILKEIHppedycikvyDPIGEEERKQFAILAKIQAEEKQRRLDEAKEKLAI 888
Cdd:COG1196   268 ELEELRLELEELELELEEAQAEEYELLAELARLEQ----------DIARLEERRRELEERLEELEEELAELEEELEELEE 337
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  889 DKEKLRLKKEALQRELEERNKAERQKK---MDDEERHREKERQKKAERDARLQFAKEnAAKLAAQEAKKDISLKSRLEQA 965
Cdd:COG1196   338 ELEELEEELEEAEEELEEAEAELAEAEealLEAEAELAEAEEELEELAEELLEALRA-AAELAAQLEELEEAEEALLERL 416
                         170       180
                  ....*....|....*....|....*..
gi 392896884  966 SMQQRERQKIDVQQAKLEAERILLLSK 992
Cdd:COG1196   417 ERLEEELEELEEALAELEEEEEEEEEA 443
PTZ00121 PTZ00121
MAEBL; Provisional
827-986 4.97e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 65.16  E-value: 4.97e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  827 KGKELRKflssiLKEIHPPEDYCIKVYDPIGEEERKQFAILAKIQAEEKQRRLDEAKEKLAIDKEKLRLKKEALQ----- 901
Cdd:PTZ00121 1291 KADEAKK-----AEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEaaeek 1365
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  902 RELEERNKAERQKKMDD-----EERHREKERQKKAERDARL--QFAKENAAKLAAQEAKKDISLKSRLEQASMQQRERQK 974
Cdd:PTZ00121 1366 AEAAEKKKEEAKKKADAakkkaEEKKKADEAKKKAEEDKKKadELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKK 1445
                         170
                  ....*....|..
gi 392896884  975 IDVQQAKLEAER 986
Cdd:PTZ00121 1446 ADEAKKKAEEAK 1457
PTZ00121 PTZ00121
MAEBL; Provisional
806-986 3.19e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 62.47  E-value: 3.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  806 QKYRQAQVRELFEHLANQTADKGKELRKflssiLKEIHPPEDycIKVYDPIGEEERKQFAILAKIQAEEKqRRLDEAKEK 885
Cdd:PTZ00121 1252 EEIRKFEEARMAHFARRQAAIKAEEARK-----ADELKKAEE--KKKADEAKKAEEKKKADEAKKKAEEA-KKADEAKKK 1323
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  886 laidKEKLRLKKEALQRELEERNKAERQKKMDDEERHREKERQKKAERDARLqfaKENAAKLAAQEAKKDISLKSRLEQA 965
Cdd:PTZ00121 1324 ----AEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEK---KKEEAKKKADAAKKKAEEKKKADEA 1396
                         170       180
                  ....*....|....*....|.
gi 392896884  966 SMQQRERQKIDVQQAKLEAER 986
Cdd:PTZ00121 1397 KKKAEEDKKKADELKKAAAAK 1417
PTZ00121 PTZ00121
MAEBL; Provisional
806-987 6.97e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 61.31  E-value: 6.97e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  806 QKYRQAQVRELFEHLANQTADKGKELRKflSSILKEIhppedycikvydpigeeERKQFAILAKIQAEEKQRRLDEAKEK 885
Cdd:PTZ00121 1555 EELKKAEEKKKAEEAKKAEEDKNMALRK--AEEAKKA-----------------EEARIEEVMKLYEEEKKMKAEEAKKA 1615
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  886 laidkEKLRLKKEALQRELEERNKAERQKKMDDEERhREKERQKKAERDARLQFA----KENAAKLAAQEAKKDISLKSR 961
Cdd:PTZ00121 1616 -----EEAKIKAEELKKAEEEKKKVEQLKKKEAEEK-KKAEELKKAEEENKIKAAeeakKAEEDKKKAEEAKKAEEDEKK 1689
                         170       180
                  ....*....|....*....|....*.
gi 392896884  962 LEQASMQQRERQKIDVQQAKLEAERI 987
Cdd:PTZ00121 1690 AAEALKKEAEEAKKAEELKKKEAEEK 1715
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
858-990 8.22e-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: 8.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  858 EEERKQfAILAKIQAEEKQRRLDEAKEKLAIDKEKLRLKKEALQRELEERNKAERQKKMDDEERHREKERQKKAERDARL 937
Cdd:COG1196   350 EEELEE-AEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 392896884  938 QFAKENAAKLAAQEAKKDI-SLKSRLEQASMQQRERQKIDVQQAKLEAERILLL 990
Cdd:COG1196   429 ALAELEEEEEEEEEALEEAaEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
858-974 9.49e-09

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 59.82  E-value: 9.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  858 EEERKQFAILAKIQAEEKQRRLDEAKEKLAIDKEKLRLKKEALQRELEERNKAE---RQKKMDDEERHREKERQKKAERD 934
Cdd:PRK09510  135 EEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEaeaAAKAAAEAKKKAEAEAKKKAAAE 214
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 392896884  935 ARLQFAKENAAKLAAQEAKKDISLKSRLEQASMQQRERQK 974
Cdd:PRK09510  215 AKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAK 254
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
858-989 1.11e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 60.34  E-value: 1.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  858 EEERKQFAILAKI------------QAEEKQRRLDEAKEKLAIDK---EKLRLKKEALQRELEERNKAERQKKMDDEE-- 920
Cdd:COG1196   222 LKELEAELLLLKLreleaeleeleaELEELEAELEELEAELAELEaelEELRLELEELELELEEAQAEEYELLAELARle 301
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392896884  921 ---RHREKERQKKAERDARLQFAKENAAKLAAQEAKKDISLKSRLEQASMQQRERQK--IDVQQAKLEAERILL 989
Cdd:COG1196   302 qdiARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAelAEAEEALLEAEAELA 375
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
858-985 1.13e-08

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


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 59.09  E-value: 1.13e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   858 EEERKQFAILAKIQAEEKQRRLDEAKEKLAIDKEKLRLKKEALQRELEERNKAERQKKMDDEERHR--EKERQKKAERDA 935
Cdd:TIGR02794   61 PAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAkqAAEAKAKAEAEA 140
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 392896884   936 RLQfAKENAAKLAAQEAKKDislksRLEQASMQQRERQKIDVQQAKLEAE 985
Cdd:TIGR02794  141 ERK-AKEEAAKQAEEEAKAK-----AAAEAKKKAEEAKKKAEAEAKAKAE 184
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
859-986 1.58e-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: 58.78  E-value: 1.58e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   859 EERKQFAILAKIQAEEK-QRRLDEAKEKLaIDKEKLRLKKEALQRE--LEERNKAERQKKMDDE--------ERHREKER 927
Cdd:pfam13868   69 EERKRYRQELEEQIEEReQKRQEEYEEKL-QEREQMDEIVERIQEEdqAEAEEKLEKQRQLREEidefneeqAEWKELEK 147
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   928 QKKAERDAR-LQFAKENAAKLAAQEAKkdislksRLEQASMQQRERQKIDVQQAKLEAER 986
Cdd:pfam13868  148 EEEREEDERiLEYLKEKAEREEEREAE-------REEIEEEKEREIARLRAQQEKAQDEK 200
MAT1 pfam06391
CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for ...
869-994 1.63e-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: 56.87  E-value: 1.63e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   869 KIQAEEKQRRLDEAKE--KLAIDKEKLRLKKEalQRELEERNKAERQKKMD--DEERHREKERQKKAERDAR-----LQF 939
Cdd:pfam06391   60 GIDVEETEKKIEQYEKenKDLILKNKMKLSQE--EEELEELLELEKREKEErrKEEKQEEEEEKEKKEKAKQelideLMT 137
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392896884   940 AKENAAKLAAQEAKKDISLKSRLEQASM-------QQRERQKIDVQQAKLEAERILLLSKYP 994
Cdd:pfam06391  138 SNKDAEEIIAQHKKTAKKRKSERRRKLEelnrvleQKPTQFSTGIKFGQLPVPKIEEGPLYP 199
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
858-985 1.79e-08

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


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 58.70  E-value: 1.79e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   858 EEERKQFAILAKIQAEEKQRRLDE--AKEKLAIDKEKLRLKKEALQRELEE---RNKAERQKKMDDE-ERHREKERQKKA 931
Cdd:TIGR02794   73 LEQQAEEAEKQRAAEQARQKELEQraAAEKAAKQAEQAAKQAEEKQKQAEEakaKQAAEAKAKAEAEaERKAKEEAAKQA 152
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 392896884   932 ERDARLQFAKENAAKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAE 985
Cdd:TIGR02794  153 EEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAA 206
PTZ00121 PTZ00121
MAEBL; Provisional
859-981 1.88e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 60.15  E-value: 1.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  859 EERKQFAILAKIQAEEKqRRLDEAKEKLAIDKEKLRLKKEAlqrelEERNKAERQKKMDDEERHREkERQKKAERDARLQ 938
Cdd:PTZ00121 1414 AAAKKKADEAKKKAEEK-KKADEAKKKAEEAKKADEAKKKA-----EEAKKAEEAKKKAEEAKKAD-EAKKKAEEAKKAD 1486
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 392896884  939 FAKENA--AKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAK 981
Cdd:PTZ00121 1487 EAKKKAeeAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAE 1531
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
883-985 1.90e-08

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 58.66  E-value: 1.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  883 KEKLAIDKEKLRLKKEALQ-RELEERNKAERQK-KMDDEERHREKERQKKAERDARLQFAKENAAKLAAQEAKKDISLKS 960
Cdd:PRK09510   70 QQKSAKRAEEQRKKKEQQQaEELQQKQAAEQERlKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKA 149
                          90       100       110
                  ....*....|....*....|....*....|...
gi 392896884  961 -----RLEQASMQQRE---RQKIDVQQAKLEAE 985
Cdd:PRK09510  150 eaeakRAAAAAKKAAAeakKKAEAEAAKKAAAE 182
PTZ00121 PTZ00121
MAEBL; Provisional
806-985 1.91e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 59.77  E-value: 1.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  806 QKYRQAQVRELFEHLANQTADKGKELRKFLSSILKEIHP--PEDYCIKVYDPIGEEERKQFAILAKIQAEEKQRRLDEAK 883
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKlyEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKK 1640
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  884 EKLAIDKEKLRLKKEALQ---RELEERNKAERQKKMDDEERHREKERQKKAERDARlqfaKENAAKLAAQEAKKDISLKS 960
Cdd:PTZ00121 1641 KEAEEKKKAEELKKAEEEnkiKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKK----EAEEAKKAEELKKKEAEEKK 1716
                         170       180
                  ....*....|....*....|....*
gi 392896884  961 RLEQASMQQRERqKIDVQQAKLEAE 985
Cdd:PTZ00121 1717 KAEELKKAEEEN-KIKAEEAKKEAE 1740
PTZ00121 PTZ00121
MAEBL; Provisional
858-985 2.81e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 59.38  E-value: 2.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  858 EEERKqfAILAKIQAEEKqRRLDEAKEKLAIDK--EKLRLKKEALQRELEERNKAERQKKMDDEERHREKERQ----KKA 931
Cdd:PTZ00121 1454 EEAKK--AEEAKKKAEEA-KKADEAKKKAEEAKkaDEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKadeaKKA 1530
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 392896884  932 ERDARLQFAKENAAKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAE 985
Cdd:PTZ00121 1531 EEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAE 1584
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
806-986 3.00e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.18  E-value: 3.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  806 QKYRQAQvRELFEHLANQTADKGKELRKFLSSILKEIHppedycikvydpigEEERKQFAILAKIQAEEKQrrLDEAKEK 885
Cdd:COG1196   213 ERYRELK-EELKELEAELLLLKLRELEAELEELEAELE--------------ELEAELEELEAELAELEAE--LEELRLE 275
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  886 LAIDKEKLRLKKEALQRELEERNKAERQKKMDDEERHREKERQKKAERD-ARLQFAKENAAKLAAQEAKKDISLKSRLE- 963
Cdd:COG1196   276 LEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEElAELEEELEELEEELEELEEELEEAEEELEe 355
                         170       180
                  ....*....|....*....|....
gi 392896884  964 -QASMQQRERQKIDVQQAKLEAER 986
Cdd:COG1196   356 aEAELAEAEEALLEAEAELAEAEE 379
PTZ00121 PTZ00121
MAEBL; Provisional
858-985 3.36e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 59.00  E-value: 3.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  858 EEERKqfAILAKIQAEEKQRRLDEAKEKLAIDKEKLRLKKEALQRELEERNKAERQKKMDDEERHREK---------ERQ 928
Cdd:PTZ00121 1480 EEAKK--ADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKkkadelkkaEEL 1557
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392896884  929 KKAERDARLQFAK-----ENAAKLAAQEAKKdiSLKSRLEQASMQQRERQKIDVQQAKLEAE 985
Cdd:PTZ00121 1558 KKAEEKKKAEEAKkaeedKNMALRKAEEAKK--AEEARIEEVMKLYEEEKKMKAEEAKKAEE 1617
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
858-1018 4.23e-08

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


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 58.13  E-value: 4.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  858 EEERKQfailAKIQAEeKQRRLDEAKEKLAIDKEKLRLKKEALQRELEErnKAERQKKMDDEERHREKERQKKAERDARL 937
Cdd:COG3064    63 EAEQRA----AELAAE-AAKKLAEAEKAAAEAEKKAAAEKAKAAKEAEA--AAAAEKAAAAAEKEKAEEAKRKAEEEAKR 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  938 QFAKE--NAAKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAERILLLSKYPNFGKGPTAAAATRPQVTAKQV 1015
Cdd:COG3064   136 KAEEErkAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAA 215

                  ...
gi 392896884 1016 PLN 1018
Cdd:COG3064   216 LLA 218
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
859-985 4.44e-08

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 57.51  E-value: 4.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  859 EERKQFaiLAKIQAEEKQRRLDEAKEKL-AIDKEKLRLKKEALQRElEERNKAERQKKMDDEERHREKERQK-KAERDAR 936
Cdd:PRK09510   78 EEQRKK--KEQQQAEELQQKQAAEQERLkQLEKERLAAQEQKKQAE-EAAKQAALKQKQAEEAAAKAAAAAKaKAEAEAK 154
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 392896884  937 lqfAKENAAKLAAQEAKKdislKSRLEQASMQQRERQKIDVQQAKLEAE 985
Cdd:PRK09510  155 ---RAAAAAKKAAAEAKK----KAEAEAAKKAAAEAKKKAEAEAAAKAA 196
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
858-985 5.38e-08

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 57.12  E-value: 5.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  858 EEERKQFAILAKIQAEEKQRRLDEAKEKLAIDKEKLRLKKEAlQRELEERNKAERQKKMDDEERHREKERQKKAERDARL 937
Cdd:PRK09510   91 ELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQK-QAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKK 169
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 392896884  938 QfAKENAAKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAE 985
Cdd:PRK09510  170 K-AEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAK 216
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
859-988 6.38e-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: 56.85  E-value: 6.38e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   859 EERKQFaILAKIQAEEKQRRLDEAKEKLAIDKEKLRLKKEALQRELEERNKAERQKKMDDEERHREKERQKKAERD---A 935
Cdd:pfam13868  130 EEIDEF-NEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDelrA 208
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 392896884   936 RLQFA------KENAAKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAERIL 988
Cdd:pfam13868  209 KLYQEeqerkeRQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERML 267
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
858-986 1.38e-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: 55.70  E-value: 1.38e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   858 EEERKQFaiLAKIQAEEKQRRLDEAKEKLAIDK---EKLRLKKEALQRELEER---NKAERQKKMDDEERHREKERQKKA 931
Cdd:pfam13868   50 EEERERA--LEEEEEKEEERKEERKRYRQELEEqieEREQKRQEEYEEKLQEReqmDEIVERIQEEDQAEAEEKLEKQRQ 127
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 392896884   932 ERDARLQFAKENAAKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAER 986
Cdd:pfam13868  128 LREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEK 182
PTZ00121 PTZ00121
MAEBL; Provisional
858-986 1.50e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 57.07  E-value: 1.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  858 EEERKqfAILAKIQAEEKqRRLDEAKEKLAIDKEKLRLKKEALQ-RELEE-RNKAERQKKMDDEERHREKERQK-----K 930
Cdd:PTZ00121 1441 EEAKK--ADEAKKKAEEA-KKAEEAKKKAEEAKKADEAKKKAEEaKKADEaKKKAEEAKKKADEAKKAAEAKKKadeakK 1517
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 392896884  931 AERDARLQFAKENAAKLAAQEAKK--DISLKSRLEQASMQQRERQKIDVQQAKLEAER 986
Cdd:PTZ00121 1518 AEEAKKADEAKKAEEAKKADEAKKaeEKKKADELKKAEELKKAEEKKKAEEAKKAEED 1575
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
857-994 1.71e-07

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: 52.77  E-value: 1.71e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   857 GEEERKQFAILAKIQAEEKQRRLDEAKEklaidkEKLRLKKEAlqRELEERNKAERQKKMDDEERHREKERQKKAERDAr 936
Cdd:pfam11600    9 SQEEKEKQRLEKDKERLRRQLKLEAEKE------EKERLKEEA--KAEKERAKEEARRKKEEEKELKEKERREKKEKDE- 79
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392896884   937 lqfaKENAAKLAAQEAK---KDISLKSRLEQASMQQRER----QKIDVQQAKLEAERILLLSKYP 994
Cdd:pfam11600   80 ----KEKAEKLRLKEEKrkeKQEALEAKLEEKRKKEEEKrlkeEEKRIKAEKAEITRFLQKPKTQ 140
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
806-985 1.86e-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: 56.29  E-value: 1.86e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   806 QKYRQAQVRELFEHLANQTADKGKELRKFLSSILKEIhppedycikvyDPIGEEE---RKQFAILAKIQAEEKQRRLDEA 882
Cdd:pfam17380  412 QRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREM-----------ERVRLEEqerQQQVERLRQQEEERKRKKLELE 480
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   883 KEKLAiDKEKLRLKKEALQRELEERNKA----ERQKKM---DDEERHR---EKERQKKAERDARLQFAKENAAKLAaQEA 952
Cdd:pfam17380  481 KEKRD-RKRAEEQRRKILEKELEERKQAmieeERKRKLlekEMEERQKaiyEEERRREAEEERRKQQEMEERRRIQ-EQM 558
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 392896884   953 KKDISLKSRLEqASMQQRE--RQKIDVQQAKLEAE 985
Cdd:pfam17380  559 RKATEERSRLE-AMEREREmmRQIVESEKARAEYE 592
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
856-992 2.12e-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: 2.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  856 IGEEERKQFAILAKIQAEEKQRRLDEAKEKLAIDKEKLRLKKEALQRELEERNKAERQkkmddEERHREKERQKKAERDA 935
Cdd:COG1196   333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE-----ALRAAAELAAQLEELEE 407
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 392896884  936 RLQFAKENAAKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAERILLLSK 992
Cdd:COG1196   408 AEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL 464
PTZ00121 PTZ00121
MAEBL; Provisional
858-981 2.19e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 56.30  E-value: 2.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  858 EEERKqfAILAKIQAEEKqRRLDEAKEKLAIDKEKLRLKKEA--------LQRELEERNKAERQKKMDDEERHREKERQK 929
Cdd:PTZ00121 1428 EEKKK--ADEAKKKAEEA-KKADEAKKKAEEAKKAEEAKKKAeeakkadeAKKKAEEAKKADEAKKKAEEAKKKADEAKK 1504
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 392896884  930 KAERDARLQFAKENAAKLAAQEAKKdISLKSRLEQASMQQRERQKIDVQQAK 981
Cdd:PTZ00121 1505 AAEAKKKADEAKKAEEAKKADEAKK-AEEAKKADEAKKAEEKKKADELKKAE 1555
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
871-986 2.49e-07

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


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 55.43  E-value: 2.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  871 QAEEKQRRLDEAKEKLAIDKEKLRLKKEALQRELEERNKaERQKKMDDEERHREKERQKKAERDARLQFAKENAAK--LA 948
Cdd:COG3064     3 EALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEE-ERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKklAE 81
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 392896884  949 AQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAER 986
Cdd:COG3064    82 AEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEK 119
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
858-988 3.58e-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: 54.54  E-value: 3.58e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   858 EEERKQFAILAKIQAEEKQRRLDEAKEKLAIDKEKLRLKKEALQRELEERnkaERQKKMDDEERHREKERQKKAERDARL 937
Cdd:pfam13868   36 AEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEER---EQKRQEEYEEKLQEREQMDEIVERIQE 112
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 392896884   938 QFAKENAAKLAAQEAKKDIslksrLEQASMQQRERQKIDVQQAKLEAERIL 988
Cdd:pfam13868  113 EDQAEAEEKLEKQRQLREE-----IDEFNEEQAEWKELEKEEEREEDERIL 158
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
858-988 3.78e-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: 54.54  E-value: 3.78e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   858 EEERKQF-AILAKIQAEEKQRRLDEAKEKLAI---------DKEKLRLKKEALQRELEERNKAERQKKMDDEERHREKER 927
Cdd:pfam13868   97 LQEREQMdEIVERIQEEDQAEAEEKLEKQRQLreeidefneEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAERE 176
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392896884   928 QKKAERDARLQFAKENAAKLAAQEAKKDiSLKSRLEQASMQQRERQK-IDVQQAKLEAERIL 988
Cdd:pfam13868  177 EIEEEKEREIARLRAQQEKAQDEKAERD-ELRAKLYQEEQERKERQKeREEAEKKARQRQEL 237
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
858-983 3.88e-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: 54.15  E-value: 3.88e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   858 EEERKQFAILAKIQAEEKQRR--LDEAKEKLAIDkeklRLKKEALQRELEERNKAERQKKM-----DDEERHREKERQKK 930
Cdd:pfam13868  180 EEKEREIARLRAQQEKAQDEKaeRDELRAKLYQE----EQERKERQKEREEAEKKARQRQElqqarEEQIELKERRLAEE 255
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392896884   931 AERD--------ARLQFAKENAAKLAAQEAKKDISLKSRLEQAsMQQRERQKIDVQQAKLE 983
Cdd:pfam13868  256 AEREeeefermlRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQ-IEEREEQRAAEREEELE 315
PTZ00121 PTZ00121
MAEBL; Provisional
823-987 4.95e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 55.15  E-value: 4.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  823 QTADKGKELRKFLSSILKEIHPPEDYCIKVYDPIGEEERKQfailAKIQAEEKQRRLDEAKeklaidKEKLRLKKEALQR 902
Cdd:PTZ00121 1240 EEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKA----DELKKAEEKKKADEAK------KAEEKKKADEAKK 1309
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  903 ELEERNKAERQKKMDDEERHREKERQKKAERDARlqfaKENAAKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKL 982
Cdd:PTZ00121 1310 KAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKK----AAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKK 1385

                  ....*
gi 392896884  983 EAERI 987
Cdd:PTZ00121 1386 KAEEK 1390
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
869-985 5.26e-07

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 54.04  E-value: 5.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  869 KIQAEEK-QRRLDEAKEKLAIDK-EKLRLKKEALQREL----EERNKAERQKKMDDEERHREKERQKKAERDARLQFAK- 941
Cdd:PRK09510   66 RQQQQQKsAKRAEEQRKKKEQQQaEELQQKQAAEQERLkqleKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAa 145
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 392896884  942 ----ENAAKLAAQEAKKDISLKSRLEQASMQQRERQKidvQQAKLEAE 985
Cdd:PRK09510  146 kakaEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAE---AKKKAEAE 190
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
867-984 6.15e-07

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


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 52.13  E-value: 6.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  867 LAKIQAEEKQ--RRLDEAKE---------KLAIDKEKLRLKKEALQRELEERNKAERQKKmddeerhrEKERQKKAERDA 935
Cdd:COG1842    46 LAQVIANQKRleRQLEELEAeaekweekaRLALEKGREDLAREALERKAELEAQAEALEA--------QLAQLEEQVEKL 117
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392896884  936 RLQfAKENAAKLAAQEAKKDIsLKSRLEQASMQQR-----------------ER--QKIDVQQAKLEA 984
Cdd:COG1842   118 KEA-LRQLESKLEELKAKKDT-LKARAKAAKAQEKvnealsgidsddatsalERmeEKIEEMEARAEA 183
Nop53 pfam07767
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ...
858-976 7.18e-07

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: 53.45  E-value: 7.18e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   858 EEERKqfailaKIQAEEKQRRLDEAKEKLAIDKEKLRLKKEALQreleERNKAErqkkmddeeRHREKERQKKAERDARL 937
Cdd:pfam07767  206 EAEKK------RLKEEEKLERVLEKIAESAATAEAREEKRKTKA----QRNKEK---------RRKEEEREAKEEKALKK 266
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 392896884   938 QFAK-ENAAKLAAQEAKKDISLKSRLEQASMQQRERQKID 976
Cdd:pfam07767  267 KLAQlERLKEIAKEIAEKEKEREEKAEARKREKRKKKKEE 306
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
858-992 7.86e-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: 53.38  E-value: 7.86e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   858 EEERKQFAILAKIQAEEKQRRLDEAKEKLAIDKE-KLRLKKEALQRELEERNKAERQKKMDDEERHREKERQKKaerdAR 936
Cdd:pfam13868  213 EEQERKERQKEREEAEKKARQRQELQQAREEQIElKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRM----KR 288
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 392896884   937 LQFAKENAAKLAAQEAKKdisLKSRLEQASMQQRERQKIDVQQAKLEAERILLLSK 992
Cdd:pfam13868  289 LEHRRELEKQIEEREEQR---AAEREEELEEGERLREEEAERRERIEEERQKKLKE 341
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
826-985 7.87e-07

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


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 53.85  E-value: 7.87e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   826 DKGKELRKFLSSiLKEIHPPEDycikvydpigeEERKQfaiLAKIQAEEKQRRLDEAKEKLAIDKEKL-RLKKEALQREL 904
Cdd:pfam05262  191 EKGVNFRRDMTD-LKERESQED-----------AKRAQ---QLKEELDKKQIDADKAQQKADFAQDNAdKQRDEVRQKQQ 255
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   905 EERN---KAERQKKMDD----EERHREKER-QKKAER-DARLQFAKENAAKLAAQEAKkdiSLKSRLEQASMQ-QRERQK 974
Cdd:pfam05262  256 EAKNlpkPADTSSPKEDkqvaENQKREIEKaQIEIKKnDEEALKAKDHKAFDLKQESK---ASEKEAEDKELEaQKKREP 332
                          170
                   ....*....|...
gi 392896884   975 I--DVQQAKLEAE 985
Cdd:pfam05262  333 VaeDLQKTKPQVE 345
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
868-1040 1.05e-06

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


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 53.50  E-value: 1.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  868 AKIQAEEKQRRLD----EAKEKLAIDKEKLRLKKEALQRELEERNKAERQKKMDDEERHREKERQKKAERDArlqfakEN 943
Cdd:COG3064    58 REAKAEAEQRAAElaaeAAKKLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKA------EE 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  944 AAKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAERILLLSKYPNFGKGPTAAAATRPQVTAKQVPLNPYGVS 1023
Cdd:COG3064   132 EAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAA 211
                         170
                  ....*....|....*..
gi 392896884 1024 SFGVAQAIIVPDNNAQR 1040
Cdd:COG3064   212 ADAALLALAVAARAAAA 228
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
858-989 1.36e-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: 50.04  E-value: 1.36e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   858 EEERKqfaILAkiqaeEKQRRLDEAKEklaidkeklRLKKEALQRELEERNKAERQKKMDDEERHR--EKERQKKAERda 935
Cdd:pfam05672   10 EEAAR---ILA-----EKRRQAREQRE---------REEQERLEKEEEERLRKEELRRRAEEERARreEEARRLEEER-- 70
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 392896884   936 rlQFAKENAAKLAAQEAKKDisLKSRLEQASMQQRERQKIDVqQAKLEAERILL 989
Cdd:pfam05672   71 --RREEEERQRKAEEEAEER--EQREQEEQERLQKQKEEAEA-KAREEAERQRQ 119
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
858-961 1.41e-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: 53.03  E-value: 1.41e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   858 EEERKQFAIL------AKIQAEEKQRRLDEAKEKLAIDKEKLRLKKEALQRELEERnKAERQKK---MDDEERHREKERQ 928
Cdd:pfam15709  405 EEERKQRLQLqaaqerARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQ-LAEEQKRlmeMAEEERLEYQRQK 483
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 392896884   929 KKAERDARLQFAK-----ENAAKLAAQEAKKDISLKSR 961
Cdd:pfam15709  484 QEAEEKARLEAEErrqkeEEAARLALEEAMKQAQEQAR 521
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
856-999 1.52e-06

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 53.29  E-value: 1.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  856 IGEEERKQFAILAKiqAEEKQRRLDEAKEKLAIDKEKLRLKKEALQRELEERNKAERQKKMDDEERHREKERQKKAERDA 935
Cdd:PRK00409  511 IGEDKEKLNELIAS--LEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADE 588
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392896884  936 RLQFAKE-NAAKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKL--EAERIlllsKYPNFG-KG 999
Cdd:PRK00409  589 IIKELRQlQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEElkVGDEV----KYLSLGqKG 652
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
858-1015 1.58e-06

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


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 53.12  E-value: 1.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  858 EEERKQFAILAKIQAEEKQRRLD-EAKEKLAIDKEKLRLKKEALQRELEE---RNKAERQKK------------------ 915
Cdd:COG3064     6 EEKAAEAAAQERLEQAEAEKRAAaEAEQKAKEEAEEERLAELEAKRQAEEearEAKAEAEQRaaelaaeaakklaeaeka 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  916 MDDEERHREKER---QKKAERDARLQFAKENAAKLAAQEAKKDISlksrlEQASMQQRERQKIDVQQAKLEAERILLLSK 992
Cdd:COG3064    86 AAEAEKKAAAEKakaAKEAEAAAAAEKAAAAAEKEKAEEAKRKAE-----EEAKRKAEEERKAAEAEAAAKAEAEAARAA 160
                         170       180
                  ....*....|....*....|...
gi 392896884  993 YPNFGKGPTAAAATRPQVTAKQV 1015
Cdd:COG3064   161 AAAAAAAAAAAARAAAGAAAALV 183
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
858-986 1.82e-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: 53.20  E-value: 1.82e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   858 EEERKQfailaKIQAEEKQRRLDEAK-EKLAIDKEKLRLKKEALQRELEERNKAERQKKMDDEERHREKERQKKAERDAR 936
Cdd:pfam17380  399 EAARKV-----KILEEERQRKIQQQKvEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERK 473
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392896884   937 ---LQFAKENAAKLAAQEAKKDI---SLKSRlEQASMQQRERQKI------DVQQAKLEAER 986
Cdd:pfam17380  474 rkkLELEKEKRDRKRAEEQRRKIlekELEER-KQAMIEEERKRKLlekemeERQKAIYEEER 534
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
871-985 3.80e-06

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 51.41  E-value: 3.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  871 QAEEKQRRLDEAKEKLAIDKEKlRLKKEALQRElEERNKAERQKKMDDEERHREKERQK-----KAERDARLQfakENAA 945
Cdd:COG2268   225 EAELEQEREIETARIAEAEAEL-AKKKAEERRE-AETARAEAEAAYEIAEANAEREVQRqleiaEREREIELQ---EKEA 299
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 392896884  946 KLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAE 985
Cdd:COG2268   300 EREEAELEADVRKPAEAEKQAAEAEAEAEAEAIRAKGLAE 339
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
858-986 4.51e-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: 4.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  858 EEERKQFAILAKIQAEEKQRRLDEAKEKLAidkEKLRLKKEALQRELEERNKA-----ERQKKMDDEERHREKERQKKAE 932
Cdd:COG1196   339 LEELEEELEEAEEELEEAEAELAEAEEALL---EAEAELAEAEEELEELAEELlealrAAAELAAQLEELEEAEEALLER 415
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 392896884  933 RDARLQFAKENAAKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAER 986
Cdd:COG1196   416 LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
PTZ00121 PTZ00121
MAEBL; Provisional
858-986 5.09e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.07  E-value: 5.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  858 EEERKQFAILAKiQAEEKQRRLDEAKEKLAIDK---EKLRLKKEALQRELEERNKAERQKKMDDEERHREKERQKKAERD 934
Cdd:PTZ00121 1670 AEEDKKKAEEAK-KAEEDEKKAAEALKKEAEEAkkaEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEE 1748
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 392896884  935 ARLQFAKEN-AAKLAAQEAKKdiSLKSRLEQASMQQRERQKIDvQQAKLEAER 986
Cdd:PTZ00121 1749 AKKDEEEKKkIAHLKKEEEKK--AEEIRKEKEAVIEEELDEED-EKRRMEVDK 1798
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
868-1034 5.70e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 50.98  E-value: 5.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  868 AKIQAEEKQRRLDEAKEKLAIDKEKLRLKKEALQREleernKAERQKKMDDEERHREKERQKKAERDARLQfAKENAAKL 947
Cdd:COG3883   141 DKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ-----QAEQEALLAQLSAEEAAAEAQLAELEAELA-AAEAAAAA 214
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  948 AAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAERILLLSKYPNFGKGPTAAAATRPQVTAKQVPLNPYGVSSFGV 1027
Cdd:COG3883   215 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGG 294

                  ....*..
gi 392896884 1028 AQAIIVP 1034
Cdd:COG3883   295 GGGAASG 301
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
795-985 8.45e-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: 51.13  E-value: 8.45e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   795 VREMDHCIYWIQKY-RQAQVRELFEHLANQTADKGKELRKFLSSILKE---IHPPEDYCIKVYDPIGEEERKQFaILAKI 870
Cdd:pfam02463  229 LDYLKLNEERIDLLqELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEeekEKKLQEEELKLLAKEEEELKSEL-LKLER 307
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   871 QAEEKQRRLDEAKEKLA-IDKEKLRLKKEALQRELE----ERNKAERQKKMDDEERHREKERQKKAERDARL----QFAK 941
Cdd:pfam02463  308 RKVDDEEKLKESEKEKKkAEKELKKEKEEIEELEKElkelEIKREAEEEEEEELEKLQEKLEQLEEELLAKKklesERLS 387
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 392896884   942 ENAAKLAAQEAKKDISLKSRLEQAsmqQRERQKIDVQQAKLEAE 985
Cdd:pfam02463  388 SAAKLKEEELELKSEEEKEAQLLL---ELARQLEDLLKEEKKEE 428
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
858-985 9.14e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 50.29  E-value: 9.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  858 EEERKQFAILAKIQAE--EKQRRLDEAKEKLAIDKEKLRLKK---EALQRELEERNK--AERQKKMDDEERHREKERQKK 930
Cdd:COG4372    31 EQLRKALFELDKLQEEleQLREELEQAREELEQLEEELEQARselEQLEEELEELNEqlQAAQAELAQAQEELESLQEEA 110
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 392896884  931 AERDARLQFAKENAAKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAE 985
Cdd:COG4372   111 EELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
858-985 9.18e-06

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


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 50.72  E-value: 9.18e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   858 EEERKQfailakiqAEEKQRRLDEAKEKLAID----KEKLRLKK-----EALQRELEERNKAeRQKKMDDEERHREKE-- 926
Cdd:pfam15709  358 EEQRRL--------QQEQLERAEKMREELELEqqrrFEEIRLRKqrleeERQRQEEEERKQR-LQLQAAQERARQQQEef 428
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392896884   927 RQKKAERDARLQfakENAAKLAAQEAKKDISLKSRL--EQAS-MQQRERQKIDVQQAKLEAE 985
Cdd:pfam15709  429 RRKLQELQRKKQ---QEEAERAEAEKQRQKELEMQLaeEQKRlMEMAEEERLEYQRQKQEAE 487
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
873-986 1.09e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.71  E-value: 1.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  873 EEKQRRLDEAKEKLAidkeklRLkkEALQRELE--------ERNKAERQKKMDDEERHREKERQKKAERDARLQFAKENA 944
Cdd:COG1196   175 EEAERKLEATEENLE------RL--EDILGELErqleplerQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEA 246
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 392896884  945 AKLAAQEAKKDISLKSRLEQASMQQrERQKIDVQQAKLEAER 986
Cdd:COG1196   247 ELEELEAELEELEAELAELEAELEE-LRLELEELELELEEAQ 287
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
868-985 1.13e-05

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


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 49.84  E-value: 1.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   868 AKIQAEEKQRRLDEAKEKlaiDKEKLRLKKEALQ-RELEERNKAE--RQKKMDD-----------EERHREKERQKKAER 933
Cdd:TIGR02794   46 GAVAQQANRIQQQKKPAA---KKEQERQKKLEQQaEEAEKQRAAEqaRQKELEQraaaekaakqaEQAAKQAEEKQKQAE 122
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 392896884   934 DARLQFAKENAAKLAAQEAKKdislksRLEQASMQQRERQKIDVQ-QAKLEAE 985
Cdd:TIGR02794  123 EAKAKQAAEAKAKAEAEAERK------AKEEAAKQAEEEAKAKAAaEAKKKAE 169
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
868-989 1.28e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 49.52  E-value: 1.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  868 AKIQAEEKQRRLDEAKEKLAIDKEKLRLKKEALQRELEERNKAERQkkMDDEERHREKERQKKAERDARLQFAKENAAKL 947
Cdd:COG4372    57 AREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEE--LESLQEEAEELQEELEELQKERQDLEQQRKQL 134
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 392896884  948 AAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAERILL 989
Cdd:COG4372   135 EAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAL 176
RRP36 pfam06102
rRNA biogenesis protein RRP36; RRP36 is involved in the early processing steps of the pre-rRNA.
861-960 1.40e-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: 47.17  E-value: 1.40e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   861 RKQFAILAKIQAEEKQrrldEAKEKLaiDKEKLRLKKEALQRELEERNKAERQKKMDDEERHREKERqKKAERDARLQ-- 938
Cdd:pfam06102   48 RKNYGFLDEYRKKEIE----ELKKQL--KKTKDPEEKEELKRTLQSMESRLKAKKRKDREREVLKEH-KKEEKEKVKQgk 120
                           90       100
                   ....*....|....*....|....*
gi 392896884   939 ---FAKENAAKLAAQEAKKDiSLKS 960
Cdd:pfam06102  121 kpfYLKKSEKKKLLLKEKFE-ELKK 144
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
858-1012 1.45e-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: 50.45  E-value: 1.45e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   858 EEERKQFAILAKIQAEEKQRRldeakEKLAIDKEKLrLKKEALQRELEER---------NKAERQKK-----MDDEERHR 923
Cdd:TIGR02169  180 EEVEENIERLDLIIDEKRQQL-----ERLRREREKA-ERYQALLKEKREYegyellkekEALERQKEaierqLASLEEEL 253
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   924 EK---ERQKKAER-DARLQFAKENAAKLAAQ------EAKKDI-SLKSRLEQA----SMQQRERQKIDVQQAKLEAERIL 988
Cdd:TIGR02169  254 EKlteEISELEKRlEEIEQLLEELNKKIKDLgeeeqlRVKEKIgELEAEIASLersiAEKERELEDAEERLAKLEAEIDK 333
                          170       180
                   ....*....|....*....|....
gi 392896884   989 LLSKYPNFGKGPTAAAATRPQVTA 1012
Cdd:TIGR02169  334 LLAEIEELEREIEEERKRRDKLTE 357
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
869-992 1.59e-05

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: 1.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  869 KIQAEEKQRRLDEAKekLAIDKEKLRLKKEALQRELEERNKAERQKKMDDEERHREKERQKKAERDARLqfakeNAAKLA 948
Cdd:COG1196   217 ELKEELKELEAELLL--LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL-----EEAQAE 289
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 392896884  949 AQEAKKDISlksRLEQASMQQRERQK-IDVQQAKLEAERILLLSK 992
Cdd:COG1196   290 EYELLAELA---RLEQDIARLEERRReLEERLEELEEELAELEEE 331
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
814-984 1.63e-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: 50.07  E-value: 1.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   814 RELFEHLAN-QTADKGKE-LRKFLSSILKEIHPPEDYCIKVYDPIGEEERKQFAILAKIQA--EEKQRRLDEAKEKLAID 889
Cdd:TIGR02169  223 YEGYELLKEkEALERQKEaIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDlgEEEQLRVKEKIGELEAE 302
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   890 KEKLRLKKEALQRELEErnkAERQKKMDDEERHREKERQKKAERDARlQFAKENAAKLAAQEAKKDI--SLKSRLEQASM 967
Cdd:TIGR02169  303 IASLERSIAEKERELED---AEERLAKLEAEIDKLLAEIEELEREIE-EERKRRDKLTEEYAELKEEleDLRAELEEVDK 378
                          170
                   ....*....|....*...
gi 392896884   968 QQRE-RQKIDVQQAKLEA 984
Cdd:TIGR02169  379 EFAEtRDELKDYREKLEK 396
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
864-992 2.13e-05

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 48.76  E-value: 2.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   864 FAILAKIQAEEKQRRLDEAKEKLAIDK--EKLRLKKEALQRELEERNKAERQK-KMDDEERHREKERQKKAERDARLQFA 940
Cdd:pfam13868   21 NKERDAQIAEKKRIKAEEKEEERRLDEmmEEERERALEEEEEKEEERKEERKRyRQELEEQIEEREQKRQEEYEEKLQER 100
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 392896884   941 KENAAKLAAQEAKkdislksrlEQASMQQRERQKIDVQQAKLEAERILLLSK 992
Cdd:pfam13868  101 EQMDEIVERIQEE---------DQAEAEEKLEKQRQLREEIDEFNEEQAEWK 143
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
873-986 2.23e-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: 45.68  E-value: 2.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   873 EEKQRRLDEAKEKLAIDKEKLRLKKEALQRELEERNKAERQKKMDDEERHR-EKERQKKAERDARLQFAKENAAK----L 947
Cdd:pfam20492    2 EEAEREKQELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERlEQKRQEAEEEKERLEESAEMEAEekeqL 81
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 392896884   948 AAQEAKKDiSLKSRLEQASmqqrERQKIDVQQAKLEAER 986
Cdd:pfam20492   82 EAELAEAQ-EEIARLEEEV----ERKEEEARRLQEELEE 115
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
802-993 2.45e-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: 49.58  E-value: 2.45e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   802 IYWIQKY-RQAQVRELFEHLANQTADKGKELRKFLSSILKEIHPPEDYCIKVydpiGEEERKQFAILAKI-QAEEKQRRL 879
Cdd:pfam02463  166 RLKRKKKeALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKE----KLELEEEYLLYLDYlKLNEERIDL 241
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   880 DEAK-----EKLAIDKEKLRLKKEALQRELEERNKAERQKKMDDEER-----HREKERQKKAERDARLQFAKENAAKLAA 949
Cdd:pfam02463  242 LQELlrdeqEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELkllakEEEELKSELLKLERRKVDDEEKLKESEK 321
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 392896884   950 QEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAERILLLSKY 993
Cdd:pfam02463  322 EKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQ 365
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
867-987 2.53e-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: 47.37  E-value: 2.53e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   867 LAKIQAEEKQ--RRLDEAKEKLAIDKEK----LRLKKEALQRE-LEERNKAERQKkmddEERHREKERQKKAERDARLQF 939
Cdd:pfam04012   45 LAQTIARQKQleRRLEQQTEQAKKLEEKaqaaLTKGNEELAREaLAEKKSLEKQA----EALETQLAQQRSAVEQLRKQL 120
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 392896884   940 AKeNAAKLAAQEAKKDIsLKSRLEQASMQQ---RERQKIDVQQAKLEAERI 987
Cdd:pfam04012  121 AA-LETKIQQLKAKKNL-LKARLKAAKAQEavqTSLGSLSTSSATDSFERI 169
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
858-944 2.92e-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: 2.92e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   858 EEERKQfailakiqAEEKQRRLDEAKEKLAIDKEKLRLKKEalqRELEERNKAERQKKMDDEERHR-EKERQKKAERDAR 936
Cdd:pfam20492   40 EEERRQ--------AEEEAERLEQKRQEAEEEKERLEESAE---MEAEEKEQLEAELAEAQEEIARlEEEVERKEEEARR 108

                   ....*...
gi 392896884   937 LQFAKENA 944
Cdd:pfam20492  109 LQEELEEA 116
MT pfam12777
Microtubule-binding stalk of dynein motor; the 380 kDa motor unit of dynein belongs to the AAA ...
867-952 3.46e-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: 48.15  E-value: 3.46e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   867 LAKIQAEEKQrrLDEAKEKLAIDKEKLRLKKEALQRELE----ERNKAERQKKMDDEERHRE-------KERQKKAERDa 935
Cdd:pfam12777    7 LLKLHSTAAQ--VDDLKAKLAAQEAELKQKNEDADKLIQvvgiEADKVSKEKAIADEEEQKVavimkevKEKQKACEED- 83
                           90
                   ....*....|....*..
gi 392896884   936 rlqFAKENAAKLAAQEA 952
Cdd:pfam12777   84 ---LAKAEPALLAAQAA 97
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
855-997 3.61e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.91  E-value: 3.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  855 PIGEEERKQfaILAKIQAEEKqrRLDEAKEKLAIDKEKLRLKKEALQRELEERNKAERQKKMDDEERHREKERQK----K 930
Cdd:PRK03918  444 ELTEEHRKE--LLEEYTAELK--RIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKynleE 519
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392896884  931 AERDAR-LQFAKENAAKLaaqeaKKDI-SLKSRLEQASMQQRERQKIDVQQAKLEAERILLLSKYPNFG 997
Cdd:PRK03918  520 LEKKAEeYEKLKEKLIKL-----KGEIkSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELG 583
PTZ00121 PTZ00121
MAEBL; Provisional
806-986 3.73e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.98  E-value: 3.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  806 QKYRQAQVRELFEHLANQTADKGKELRKFLSSILK--EIHPPEDYciKVYDPIGEEERKQFAILAKiQAEEKQRRlDEAK 883
Cdd:PTZ00121 1477 KKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKadEAKKAEEA--KKADEAKKAEEAKKADEAK-KAEEKKKA-DELK 1552
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  884 EklaidKEKLRLKKEalQRELEERNKAERQKKMddEERHREKERQKKAERDARLQFAKENAAKLAAQEAKKDISLKSRLE 963
Cdd:PTZ00121 1553 K-----AEELKKAEE--KKKAEEAKKAEEDKNM--ALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAE 1623
                         170       180
                  ....*....|....*....|...
gi 392896884  964 QASMQQRERQKIDVQQAKLEAER 986
Cdd:PTZ00121 1624 ELKKAEEEKKKVEQLKKKEAEEK 1646
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
858-968 3.76e-05

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 48.26  E-value: 3.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  858 EEERKQFAILAKIQAEEKQRRLDEAKEKLAIDKEKLRLKKEALQR---ELEERNKAERQKKMDDEERhrekerqKKAERD 934
Cdd:PRK09510  150 EAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKaaaEAKKKAEAEAKKKAAAEAK-------KKAAAE 222
                          90       100       110
                  ....*....|....*....|....*....|....
gi 392896884  935 ARLQFAKENAAKLAAQEAKKDISLKSRLEQASMQ 968
Cdd:PRK09510  223 AKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAA 256
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
791-986 4.07e-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: 49.02  E-value: 4.07e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   791 LESHVREMDHCIYWIQ---KYRQAQVRELFEHLANQTADKGK-ELRKF-LSSILKEIHppEDYCIKvydpigEEERkqfa 865
Cdd:pfam01576   80 LESRLEEEEERSQQLQnekKKMQQHIQDLEEQLDEEEAARQKlQLEKVtTEAKIKKLE--EDILLL------EDQN---- 147
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   866 ilAKIQAEEKQ--RRLDEAKEKLAIDKEK------LRLKKEALQRELEERNKAERQKKMDDEERHREKERQKKAERD--A 935
Cdd:pfam01576  148 --SKLSKERKLleERISEFTSNLAEEEEKakslskLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEqiA 225
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392896884   936 RLQfakENAAKLAAQEAKKDISLKS---RLEQASMQQRERQK--------IDVQQAKLEAER 986
Cdd:pfam01576  226 ELQ---AQIAELRAQLAKKEEELQAalaRLEEETAQKNNALKkireleaqISELQEDLESER 284
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
869-989 4.98e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.39  E-value: 4.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  869 KIQAEeKQRRLDEAKEKL-AIDKEKLRLKKEALQRELE---------ERNKAERQKKMDDEERHREKERQKKAERDARLQ 938
Cdd:COG1196   206 ERQAE-KAERYRELKEELkELEAELLLLKLRELEAELEeleaeleelEAELEELEAELAELEAELEELRLELEELELELE 284
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 392896884  939 FAKENAAKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAERILL 989
Cdd:COG1196   285 EAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEEL 335
CCDC66 pfam15236
Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil ...
861-974 5.08e-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: 45.56  E-value: 5.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   861 RKQFAILAKIQAEEKQRRLDEAKEKLAIDKEKLRLKKeaLQRELEErnkaERQKKMDDEE-----RHREKErQKKAERDA 935
Cdd:pfam15236   33 RGQNALLDPAQLEERERKRQKALEHQNAIKKQLEEKE--RQKKLEE----ERRRQEEQEEeerlrREREEE-QKQFEEER 105
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 392896884   936 RLQFAKENAAKLAAQEakkdisLKSRLEQASMQ-QRERQK 974
Cdd:pfam15236  106 RKQKEKEEAMTRKTQA------LLQAMQKAQELaQRLKQE 139
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
858-980 5.39e-05

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


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 47.53  E-value: 5.39e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   858 EEERKQFAILAKiQAEEKQRrldeAKEKLAIDKEKLRLKKealQRELEERNKAERQKKMDDEERHREKERQK-KAERDA- 935
Cdd:TIGR02794  139 EAERKAKEEAAK-QAEEEAK----AKAAAEAKKKAEEAKK---KAEAEAKAKAEAEAKAKAEEAKAKAEAAKaKAAAEAa 210
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 392896884   936 -RLQFAKENAAKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQA 980
Cdd:TIGR02794  211 aKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAA 256
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
882-992 5.42e-05

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


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 48.11  E-value: 5.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  882 AKEKLAIDKEKLRLKKEALQRELEERNKAERQKKMDDE---ERHREKERQKKAERDARLQFA--KENAAKLAAQEAKKdi 956
Cdd:COG3064     1 AQEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEaeeERLAELEAKRQAEEEAREAKAeaEQRAAELAAEAAKK-- 78
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 392896884  957 slKSRLEQASMQQRERQKIDVQQAKLEAERILLLSK 992
Cdd:COG3064    79 --LAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEK 112
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
806-992 5.74e-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: 48.43  E-value: 5.74e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   806 QKYRQAQVRELF-----EHLANQTADKGKELRKFLSSILKEIHPPEDYCIKVYDPIGEEE----RKQFAILAKIQAEEKQ 876
Cdd:pfam02463  300 SELLKLERRKVDdeeklKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEelekLQEKLEQLEEELLAKK 379
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   877 RRLDEAKEKLAIDKEKLRLKKEALQRELEERNKAERQKKMDDEERHREKERQKKAERDaRLQFAKENAAKLAAQEAKKDI 956
Cdd:pfam02463  380 KLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEE-SIELKQGKLTEEKEELEKQEL 458
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 392896884   957 SLKSRLEQASMQQRERQKIDVQQAKLEAERILLLSK 992
Cdd:pfam02463  459 KLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQK 494
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
858-938 5.94e-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: 45.03  E-value: 5.94e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   858 EEERKQFAILAKIQAEEKQRRLDEAK-----EKLAIDKEKLRLKKEALQRELEERNKAERQKKMDDE---------ERHR 923
Cdd:pfam05672   39 EEERLRKEELRRRAEEERARREEEARrleeeRRREEEERQRKAEEEAEEREQREQEEQERLQKQKEEaeakareeaERQR 118
                           90
                   ....*....|....*.
gi 392896884   924 -EKERQKKAERDARLQ 938
Cdd:pfam05672  119 qEREKIMQQEEQERLE 134
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
858-984 6.85e-05

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


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 47.64  E-value: 6.85e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   858 EEERKQFAI-LAKIQAEEKQRRLDEAKEK----LAIDKEKLRLKKEALQRELEERnkaERQKKMDDEER-HREKERQKK- 930
Cdd:pfam15709  381 EQQRRFEEIrLRKQRLEEERQRQEEEERKqrlqLQAAQERARQQQEEFRRKLQEL---QRKKQQEEAERaEAEKQRQKEl 457
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392896884   931 ----AERDARL-QFAKENaaKLAAQEAKKDISLKSRLEQASMQQRERQKIDV------QQAKLEA 984
Cdd:pfam15709  458 emqlAEEQKRLmEMAEEE--RLEYQRQKQEAEEKARLEAEERRQKEEEAARLaleeamKQAQEQA 520
PTZ00121 PTZ00121
MAEBL; Provisional
873-995 7.38e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.21  E-value: 7.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  873 EEKQRRLDEAKEKLAIDKEKLRLKKEALQRElEERNKAERQKKMDDEerhREKERQKKAERDARLQFAKENAAKLAAQEA 952
Cdd:PTZ00121 1094 EEAFGKAEEAKKTETGKAEEARKAEEAKKKA-EDARKAEEARKAEDA---RKAEEARKAEDAKRVEIARKAEDARKAEEA 1169
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 392896884  953 KKDISLKsRLEQASMQQRERQKIDVQQAKlEAERILLLSKYPN 995
Cdd:PTZ00121 1170 RKAEDAK-KAEAARKAEEVRKAEELRKAE-DARKAEAARKAEE 1210
CCDC47 pfam07946
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ...
888-974 8.85e-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: 46.79  E-value: 8.85e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   888 IDK--EKLRLKKEALQR-------ELEERNKAERQKKMddEERHREKERQKKAERDARLqfakenaAKLAAQEAKKdisl 958
Cdd:pfam07946  245 IDKlaKRAKLRPEALKKakktreeEIEKIKKAAEEERA--EEAQEKKEEAKKKEREEKL-------AKLSPEEQRK---- 311
                           90
                   ....*....|....*.
gi 392896884   959 ksrleqasMQQRERQK 974
Cdd:pfam07946  312 --------YEEKERKK 319
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
873-954 9.33e-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: 44.66  E-value: 9.33e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   873 EEKQRRLDEAKEKL------AIDKEKLRLKKEALQRELEERNK--------AERQKKMDDEERHREKERQKKAERDARLq 938
Cdd:pfam15346   37 AEVERRVEEARKIMekqvleELEREREAELEEERRKEEEERKKreelerilEENNRKIEEAQRKEAEERLAMLEEQRRM- 115
                           90
                   ....*....|....*.
gi 392896884   939 faKENAAKLAAQEAKK 954
Cdd:pfam15346  116 --KEERQRREKEEEER 129
DDRGK pfam09756
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ...
883-973 1.03e-04

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


Pssm-ID: 370664 [Multi-domain]  Cd Length: 188  Bit Score: 45.03  E-value: 1.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   883 KEKLAIdKEKLRLKKEALQRELEERNK--AERQKKMDDEERHREKERQKKAERDARLQFAKENAAKLAAQEAKKDISLKS 960
Cdd:pfam09756    8 RAKLEL-KEAKRQQREAEEEEREEREKleEKREEEYKEREEREEEAEKEKEEEERKQEEEQERKEQEEYEKLKSQFVVEE 86
                           90
                   ....*....|...
gi 392896884   961 RLEQASMQQRERQ 973
Cdd:pfam09756   87 EGTDKLSAEDESQ 99
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
786-986 1.04e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 47.37  E-value: 1.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  786 KRAIALESHVREMDHciywiqkyrqaQVRELFEHLAN---QTADKGKELRKFLSSILKEIHPPEDYCIKVYDpigeeerk 862
Cdd:PRK03918  549 EKLEELKKKLAELEK-----------KLDELEEELAEllkELEELGFESVEELEERLKELEPFYNEYLELKD-------- 609
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  863 qfailAKIQAEEKQRRLDEAKEKLAIDKEKLRLKKEALqRELeeRNKAERQKKMDDEERHREKERQ--KKAERDARLQFA 940
Cdd:PRK03918  610 -----AEKELEREEKELKKLEEELDKAFEELAETEKRL-EEL--RKELEELEKKYSEEEYEELREEylELSRELAGLRAE 681
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 392896884  941 KENAAKLaAQEAKKDIS-LKSRLEQASMQQRERQKIDVQQAKLEAER 986
Cdd:PRK03918  682 LEELEKR-REEIKKTLEkLKEELEEREKAKKELEKLEKALERVEELR 727
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
857-984 1.04e-04

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


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 46.42  E-value: 1.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  857 GEEERKQFaiLAKIQAEEKQ-RRLDEAKEKLAIDKEKLRLKKEAL---QRELEERNKAERQKKMDDEERHREKERQ--KK 930
Cdd:cd16269   168 AEEVLQEF--LQSKEAEAEAiLQADQALTEKEKEIEAERAKAEAAeqeRKLLEEQQRELEQKLEDQERSYEEHLRQlkEK 245
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 392896884  931 AERDARLQfakenaaklaAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEA 984
Cdd:cd16269   246 MEEERENL----------LKEQERALESKLKEQEALLEEGFKEQAELLQEEIRS 289
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
869-986 1.18e-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: 46.87  E-value: 1.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   869 KIQAEEKQRRLDEAKEKLAIDKEKLRLKKEALQR--------ELEERNKAE--RQKKMDDEErhrEKERQKKAERDARLQ 938
Cdd:pfam15709  337 RLRAERAEMRRLEVERKRREQEEQRRLQQEQLERaekmreelELEQQRRFEeiRLRKQRLEE---ERQRQEEEERKQRLQ 413
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 392896884   939 FAkenaaklAAQEakkdislKSRLEQASMQ------QRERQKIDVQQAKLEAER 986
Cdd:pfam15709  414 LQ-------AAQE-------RARQQQEEFRrklqelQRKKQQEEAERAEAEKQR 453
PTZ00121 PTZ00121
MAEBL; Provisional
858-985 1.20e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.44  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  858 EEERKQFAI--LAKIQAEEKQRRLDEAKEKLAIDK-EKLRLKKEAlqRELEERNKAERQKKMDDEERHREKERQKKAER- 933
Cdd:PTZ00121 1179 EAARKAEEVrkAEELRKAEDARKAEAARKAEEERKaEEARKAEDA--KKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRk 1256
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 392896884  934 --DARLQFAKENAAKLAAQEAKKDISLKSRLE--QASMQQRERQKIDVQQAKLEAE 985
Cdd:PTZ00121 1257 feEARMAHFARRQAAIKAEEARKADELKKAEEkkKADEAKKAEEKKKADEAKKKAE 1312
PRK12704 PRK12704
phosphodiesterase; Provisional
858-991 1.37e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 46.69  E-value: 1.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  858 EEERKQFAILAKIQAEE-KQRRLDEAKEKlaIDKEKLRLKKEA--------------LQRE---------LEERNKAERQ 913
Cdd:PRK12704   37 EEEAKRILEEAKKEAEAiKKEALLEAKEE--IHKLRNEFEKELrerrnelqklekrlLQKEenldrklelLEKREEELEK 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  914 KKMDDEERHRE-KERQKKAERDARLQFAK-ENAAKLAAQEAKKDI--SLKSRLE-QASMQQRERQKIDVQQAKLEAERIL 988
Cdd:PRK12704  115 KEKELEQKQQElEKKEEELEELIEEQLQElERISGLTAEEAKEILleKVEEEARhEAAVLIKEIEEEAKEEADKKAKEIL 194

                  ...
gi 392896884  989 LLS 991
Cdd:PRK12704  195 AQA 197
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
882-936 1.40e-04

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: 47.07  E-value: 1.40e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 392896884   882 AKEKLAIDKEKL--RLKKEALQRELEERNKaERQKkmdDEERHREKERQKKAERDAR 936
Cdd:pfam03154  581 AGSKLAKKREEAleKAKREAEQKAREEKER-EKEK---EKEREREREREREAERAAK 633
PTZ00121 PTZ00121
MAEBL; Provisional
823-986 1.75e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 1.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  823 QTADKGKELRKflssiLKEIHPPEDycIKVYDPIGEEERKQFAILAKIQAEEKQRRLDEAKEKLAIdkEKLRLKKEALQR 902
Cdd:PTZ00121 1531 EEAKKADEAKK-----AEEKKKADE--LKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKA--EEARIEEVMKLY 1601
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  903 ELEERNKAERQKKMDD-----EERHREKERQKKAERDAR-----------LQFAKENAAKLAAQEAKKDISLKSRLEQAS 966
Cdd:PTZ00121 1602 EEEKKMKAEEAKKAEEakikaEELKKAEEEKKKVEQLKKkeaeekkkaeeLKKAEEENKIKAAEEAKKAEEDKKKAEEAK 1681
                         170       180
                  ....*....|....*....|
gi 392896884  967 MQQRERQKIDVQQAKLEAER 986
Cdd:PTZ00121 1682 KAEEDEKKAAEALKKEAEEA 1701
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
871-989 2.04e-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: 45.80  E-value: 2.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   871 QAEEKQRRLDEAKEKLAIDKEKLRLKKEALQRELEERNKAERQKKMDD------------EERHREKERQKKAERDarlQ 938
Cdd:pfam15558   66 EKEQRKARLGREERRRADRREKQVIEKESRWREQAEDQENQRQEKLERarqeaeqrkqcqEQRLKEKEEELQALRE---Q 142
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 392896884   939 FAKENAAKLAAQEAKKdiSLKSRLEQASMQQRERQKIDVQQAKL-------EAERILL 989
Cdd:pfam15558  143 NSLQLQERLEEACHKR--QLKEREEQKKVQENNLSELLNHQARKvlvdcqaKAEELLR 198
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
790-971 2.07e-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: 46.32  E-value: 2.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   790 ALESHVREMdhciywiqkyrQAQVRELFEHLanQTADKGKeLRkfLSSILKEIHPPEDYCIKVYDPIGEEERKQFA---- 865
Cdd:pfam01576  689 ALEQQVEEM-----------KTQLEELEDEL--QATEDAK-LR--LEVNMQALKAQFERDLQARDEQGEEKRRQLVkqvr 752
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   866 -ILAKIQAEEKQRRLD-EAKEKLAIDKEKLRLKKEALQRELEERNKAER--QKKMDDEERHREKERqkkAERDARLQFAK 941
Cdd:pfam01576  753 eLEAELEDERKQRAQAvAAKKKLELDLKELEAQIDAANKGREEAVKQLKklQAQMKDLQRELEEAR---ASRDEILAQSK 829
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 392896884   942 ENAAKLAAQEA-----KKDISLKSRLEQASMQQRE 971
Cdd:pfam01576  830 ESEKKLKNLEAellqlQEDLAASERARRQAQQERD 864
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
850-992 2.16e-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: 46.59  E-value: 2.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   850 IKVYDPIGEEERKQFAIlaKIQAE--EKQRRLDEAKEKLAIDKEKLRLkkEALQRELEERNKAERQKkmddEERHREKER 927
Cdd:TIGR02168  189 DRLEDILNELERQLKSL--ERQAEkaERYKELKAELRELELALLVLRL--EELREELEELQEELKEA----EEELEELTA 260
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392896884   928 QKKAER----DARLQFAKENAAKLAAQEAKKDIS-LKSRLEQASMQQRERQKIDVQQAK-LEAERILLLSK 992
Cdd:TIGR02168  261 ELQELEekleELRLEVSELEEEIEELQKELYALAnEISRLEQQKQILRERLANLERQLEeLEAQLEELESK 331
PTZ00121 PTZ00121
MAEBL; Provisional
858-985 2.76e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.29  E-value: 2.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  858 EEERKqfaILAKIQAEEKQRRLDEAKEKlaidkEKLRLKKEALQRELEERNKAERQKKMDDEERHREKERQKKAERDARL 937
Cdd:PTZ00121 1221 EDAKK---AEAVKKAEEAKKDAEEAKKA-----EEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKA 1292
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 392896884  938 QFAKENAAKLAAQEAKKDISLKSRLEQASMQQRERQKiDVQQAKLEAE 985
Cdd:PTZ00121 1293 DEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKK-KADAAKKKAE 1339
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
815-982 3.12e-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: 3.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   815 ELFEHLANQTADKGKELRKFLSSILKEIHPPEDYCIKVYDPIGEEERKQFAILAKIQAEEKQRRLDEAK--EKLAIDKEK 892
Cdd:TIGR00618  176 DQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYltQKREAQEEQ 255
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   893 LRLKKEA--LQRELEE--------------RNKAERQKKMDDEERHREKERQKKAERDARLQ-----FAKENAAKLAAQE 951
Cdd:TIGR00618  256 LKKQQLLkqLRARIEElraqeavleetqerINRARKAAPLAAHIKAVTQIEQQAQRIHTELQskmrsRAKLLMKRAAHVK 335
                          170       180       190
                   ....*....|....*....|....*....|.
gi 392896884   952 AKKDISLKSRLEQASMQQRERQKIDVQQAKL 982
Cdd:TIGR00618  336 QQSSIEEQRRLLQTLHSQEIHIRDAHEVATS 366
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
856-986 3.35e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.53  E-value: 3.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  856 IGEEERKQFAILAKIQA-EEKQRRLDEAKEKLA-IDKEKLRLKKEALQRELEERNKAERQKKMDDEERHREKERQKK--A 931
Cdd:COG4717    80 LKEAEEKEEEYAELQEElEELEEELEELEAELEeLREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEelR 159
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392896884  932 ERDARLQFAKENAAKLAAQ--EAKKDIS------LKSRLEQASMQQRERQKIDVQQAKLEAER 986
Cdd:COG4717   160 ELEEELEELEAELAELQEEleELLEQLSlateeeLQDLAEELEELQQRLAELEEELEEAQEEL 222
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
860-985 3.41e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.53  E-value: 3.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  860 ERKQFAILAKIQAEEKQRRLDEAKEKLAIDKEKLrlkkEALQRELEERNKAERQKKMDDEERHR------EKERQKKAER 933
Cdd:COG4717   115 REELEKLEKLLQLLPLYQELEALEAELAELPERL----EELEERLEELRELEEELEELEAELAElqeeleELLEQLSLAT 190
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 392896884  934 DARLQFAKENAAKLAAQEAKkdisLKSRLEQAsmqQRERQKIDVQQAKLEAE 985
Cdd:COG4717   191 EEELQDLAEELEELQQRLAE----LEEELEEA---QEELEELEEELEQLENE 235
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
873-986 3.65e-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: 45.55  E-value: 3.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   873 EEKQRRLDEAKE-KLAIDKEKLRLKKEALqrELEERNKAERQKKMDDEERHR----------------EKERQKKAERDA 935
Cdd:pfam01576  359 EELTEQLEQAKRnKANLEKAKQALESENA--ELQAELRTLQQAKQDSEHKRKklegqlqelqarlsesERQRAELAEKLS 436
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392896884   936 RLQFAKENAAKLAAQEAKKDI-------SLKSRLE--QASMQQRERQKIDV--QQAKLEAER 986
Cdd:pfam01576  437 KLQSELESVSSLLNEAEGKNIklskdvsSLESQLQdtQELLQEETRQKLNLstRLRQLEDER 498
eIF3_subunit pfam08597
Translation initiation factor eIF3 subunit; This is a family of proteins which are subunits of ...
873-960 3.77e-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: 44.21  E-value: 3.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   873 EEKQRRLDEAKEKlaidKEKLRLKKEALQRELEERNK--AERQKKMDDEERHREKERQKKAERDARLqfakENAAKL--A 948
Cdd:pfam08597   47 KEKAAKAAAAKAK----KKKKSKKQKIAEKEAERKAEeeAEEEEELTPEDEAARKLRLRKAEEESDL----ENAADLfgG 118
                           90
                   ....*....|..
gi 392896884   949 AQEAKKDISLKS 960
Cdd:pfam08597  119 AGDPTKDTDLSS 130
Caldesmon pfam02029
Caldesmon;
845-993 4.29e-04

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 45.24  E-value: 4.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   845 PEDYCIKVYDPIGEEERKQFAILAKIQAEEKQRRLDEAKEK-----LAIDKEKLRLKKEALQRELEERNKAERQKKMDDE 919
Cdd:pfam02029   45 EEDSELKPSGQGGLDEEEAFLDRTAKREERRQKRLQEALERqkefdPTIADEKESVAERKENNEEEENSSWEKEEKRDSR 124
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392896884   920 ERHREKERQKKAERDARLQfAKENAAKLAAQEAKKDislksRLEQASMQQRERQKIDVQQAKLEAERILLLSKY 993
Cdd:pfam02029  125 LGRYKEEETEIREKEYQEN-KWSTEVRQAEEEGEEE-----EDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKY 192
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
894-986 5.57e-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: 44.64  E-value: 5.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   894 RLKKEALQRELeeRNKAERQKkmdDEERHREKERQKKAERDARLQFAKENAAKLAAQEAKkdislKSRLEQasmQQRERQ 973
Cdd:pfam15558   16 RHKEEQRMREL--QQQAALAW---EELRRRDQKRQETLERERRLLLQQSQEQWQAEKEQR-----KARLGR---EERRRA 82
                           90
                   ....*....|...
gi 392896884   974 KIDVQQAKLEAER 986
Cdd:pfam15558   83 DRREKQVIEKESR 95
TAF4 pfam05236
Transcription initiation factor TFIID component TAF4 family; This region of similarity is ...
861-924 5.71e-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: 43.80  E-value: 5.71e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392896884   861 RKQFAILAKIQAEEKQRRLDEAKEKLA---------IDKEKLRLKKEAlqreleernkAERQKKMDDEERHRE 924
Cdd:pfam05236  113 RKQLKFLAQKDKEEEERRVAEEREGLLkaaksrsnqEDPEQLKLKQEA----------KEMQKEEDEKMRHRA 175
PTZ00121 PTZ00121
MAEBL; Provisional
858-987 6.09e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.13  E-value: 6.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  858 EEERKQFAILAKIQAE--EKQRRLDEAKEKlaidKEKLRLKKEAlqRELEERNKAERQKKMDDEER---HREKERQKKAE 932
Cdd:PTZ00121 1094 EEAFGKAEEAKKTETGkaEEARKAEEAKKK----AEDARKAEEA--RKAEDARKAEEARKAEDAKRveiARKAEDARKAE 1167
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  933 RDARLQFAKENAAKLAAQEAKKDISLKS-----RLEQASMQQRERQKIDVQQAKlEAERI 987
Cdd:PTZ00121 1168 EARKAEDAKKAEAARKAEEVRKAEELRKaedarKAEAARKAEEERKAEEARKAE-DAKKA 1226
YscO-like pfam16789
YscO-like protein; This family of proteins is similar to the type III secretion protein YscO. ...
875-987 6.56e-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: 42.13  E-value: 6.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   875 KQRRLDEAKEKLAIDKEKLRLKKEALQRELEERNKAERQKK---------MDD-----------EERHREKERQKKAERD 934
Cdd:pfam16789   12 KKKRVEEAEKVVKDKKRALEKEKEKLAELEAERDKVRKHKKakmqqlrdeMDRgttsdkilqmkRYIKVVKERLKQEEKK 91
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 392896884   935 ARLQFAKENAAKLAAQEAKKDISLKSRLEQASMQQRERQkidVQQAKLEAERI 987
Cdd:pfam16789   92 VQDQKEQVRTAARNLEIAREELKKKRQEVEKLEKHKKEW---VKEMKKEEEDQ 141
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
858-987 6.86e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.12  E-value: 6.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  858 EEERKQfailAKIQAEEKQRRLDEAKEKLAIDKEKLRLKKEALQRELEERNKAERQKKmddeerHREKERQKKAERDARL 937
Cdd:COG4372    65 EEELEQ----ARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELE------ELQKERQDLEQQRKQL 134
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 392896884  938 QfakENAAKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAERI 987
Cdd:COG4372   135 E---AQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEA 181
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
858-989 8.25e-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: 44.66  E-value: 8.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   858 EEERKQFAILAKiQAEEKQRRLDEAKEKLA---IDKEKLRLKKEALQRELEERNKA--ERQKKMDDEERHREKERQKKAE 932
Cdd:TIGR02168  221 ELRELELALLVL-RLEELREELEELQEELKeaeEELEELTAELQELEEKLEELRLEvsELEEEIEELQKELYALANEISR 299
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392896884   933 RDARLQFAKENAAKLAAQEAKKDISL---KSRLE--QASMQQRErQKIDVQQAKLEAERILL 989
Cdd:TIGR02168  300 LEQQKQILRERLANLERQLEELEAQLeelESKLDelAEELAELE-EKLEELKEELESLEAEL 360
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
809-990 9.37e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.99  E-value: 9.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  809 RQAQVRELFEHLANQTADKGKELRKFlsSILKEIHPPEdycikvydpigeEERKQfailAKIQAEEKQRRLDEAKEKLA- 887
Cdd:COG4717    96 ELEELEEELEELEAELEELREELEKL--EKLLQLLPLY------------QELEA----LEAELAELPERLEELEERLEe 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  888 -----IDKEKLRLKKEALQRELEE---RNKAERQKKMDDEERHREKERQKKAERDARLQFAKENAAKLAAQEAkkdislk 959
Cdd:COG4717   158 lreleEELEELEAELAELQEELEElleQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE------- 230
                         170       180       190
                  ....*....|....*....|....*....|.
gi 392896884  960 sRLEQASMQQRERQKIDVQQAKLEAERILLL 990
Cdd:COG4717   231 -QLENELEAAALEERLKEARLLLLIAAALLA 260
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
813-985 1.02e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.28  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  813 VRELFEHLANQTAdKGKELRKFLSSILKEIHPPEDYcIKVYDPIG------EEERKQFAILAKIQAEEKQRRLDEAKEKL 886
Cdd:PRK03918  326 IEERIKELEEKEE-RLEELKKKLKELEKRLEELEER-HELYEEAKakkeelERLKKRLTGLTPEKLEKELEELEKAKEEI 403
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  887 AIDKEKLRLKKEALQRELEERNKA-ERQKK-----------MDDEERHR---------EKERQKKAERDARLQFAKENAA 945
Cdd:PRK03918  404 EEEISKITARIGELKKEIKELKKAiEELKKakgkcpvcgreLTEEHRKElleeytaelKRIEKELKEIEEKERKLRKELR 483
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 392896884  946 KL--AAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAE 985
Cdd:PRK03918  484 ELekVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAE 525
CCDC34 pfam13904
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ...
858-974 1.16e-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: 42.38  E-value: 1.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   858 EEERKQfailaKIQA--EEKQRRLDEAKEKLAIDKEKLrlkKEALQRELEERNKAERQKKMDDEERHREKER----QKKA 931
Cdd:pfam13904   65 QRQRQK-----ELQAqkEEREKEEQEAELRKRLAKEKY---QEWLQRKARQQTKKREESHKQKAAESASKSLakpeRKVS 136
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 392896884   932 ERDARLQFAKENAAKLAAQEAKKdisLKSRLEQASMQQRERQK 974
Cdd:pfam13904  137 QEEAKEVLQEWERKKLEQQQRKR---EEEQREQLKKEEEEQER 176
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
857-985 1.17e-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: 43.89  E-value: 1.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   857 GEEERKQFAILAKIQAEEKQRRLDEAKEKLAIDKEKLRLKKEALQRELEE-----RNKAER----QKKMDDEERHREKER 927
Cdd:TIGR02168  765 ELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLlneeaANLRERleslERRIAATERRLEDLE 844
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 392896884   928 QKKAERDARLQFAKENAAKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAE 985
Cdd:TIGR02168  845 EQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEE 902
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
868-986 1.18e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.35  E-value: 1.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  868 AKIQAEEKQRRLDEAKEKLaidkEKLRLKKEALQRELEERNKaERQKKmddeerhrekeRQKKAERDARLQFAKENAAKL 947
Cdd:COG4372    36 ALFELDKLQEELEQLREEL----EQAREELEQLEEELEQARS-ELEQL-----------EEELEELNEQLQAAQAELAQA 99
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 392896884  948 AAQeakkdisLKSRLEQASMQQRERQKIDVQQAKLEAER 986
Cdd:COG4372   100 QEE-------LESLQEEAEELQEELEELQKERQDLEQQR 131
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
856-951 1.31e-03

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 43.96  E-value: 1.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  856 IGEEERKQFAILAKIQAEEKQRRLdEAKEKLAIDKEKL-RLKKEALQRELEERNKAERQKKMDDEERHREKERQKKAERD 934
Cdd:PTZ00266  440 IEKENAHRKALEMKILEKKRIERL-EREERERLERERMeRIERERLERERLERERLERDRLERDRLDRLERERVDRLERD 518
                          90
                  ....*....|....*..
gi 392896884  935 aRLQFAKENAAKLAAQE 951
Cdd:PTZ00266  519 -RLEKARRNSYFLKGME 534
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
856-957 1.34e-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: 43.21  E-value: 1.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  856 IGEEERKQFAILAKIQAE--EKQRRLDEAKEKLAIDKEKLRLKKEALQRELEERNKAerQKKMDDEERHREKERQKKAER 933
Cdd:COG4942   144 LAPARREQAEELRADLAElaALRAELEAERAELEALLAELEEERAALEALKAERQKL--LARLEKELAELAAELAELQQE 221
                          90       100
                  ....*....|....*....|....
gi 392896884  934 DARLQFAKENAAKLAAQEAKKDIS 957
Cdd:COG4942   222 AEELEALIARLEAEAAAAAERTPA 245
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
888-986 1.47e-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: 42.91  E-value: 1.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   888 IDKEKLRLKKEALQRELEERNKAERQKKMDDEERHREKERQKKAE----RDARLQFAKENAAKLAAQEAKKDISLKSRLE 963
Cdd:TIGR02794   43 VDPGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEqarqKELEQRAAAEKAAKQAEQAAKQAEEKQKQAE 122
                           90       100
                   ....*....|....*....|...
gi 392896884   964 QASMQQRERQKidvqqAKLEAER 986
Cdd:TIGR02794  123 EAKAKQAAEAK-----AKAEAEA 140
PRK05035 PRK05035
electron transport complex protein RnfC; Provisional
868-985 1.53e-03

electron transport complex protein RnfC; Provisional


Pssm-ID: 235334 [Multi-domain]  Cd Length: 695  Bit Score: 43.40  E-value: 1.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  868 AKIQA-EEKQRRLDEAKEKLAidkeklrLKKEALQREleernKAERqkkmddEERHREKERQKKAERDARLQFAKE--NA 944
Cdd:PRK05035  436 AEIRAiEQEKKKAEEAKARFE-------ARQARLERE-----KAAR------EARHKKAAEARAAKDKDAVAAALArvKA 497
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 392896884  945 AKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAE 985
Cdd:PRK05035  498 KKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQ 538
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
852-988 1.55e-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: 40.50  E-value: 1.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  852 VYDPIGE--EERKQfailaKIQAEekqrrLDEAKEKlaidKEKLRLKKEALQRELEERnKAERQKKMDDEERHREKERQK 929
Cdd:cd06503    20 LWKPILKalDEREE-----KIAES-----LEEAEKA----KEEAEELLAEYEEKLAEA-RAEAQEIIEEARKEAEKIKEE 84
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 392896884  930 KAERdarlqfAKENAAKLAAQeAKKDIslksRLEQASMQQRERQKIdVQQAKLEAERIL 988
Cdd:cd06503    85 ILAE------AKEEAERILEQ-AKAEI----EQEKEKALAELRKEV-ADLAVEAAEKIL 131
PRK12705 PRK12705
hypothetical protein; Provisional
858-986 1.58e-03

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 43.16  E-value: 1.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  858 EEERKQFAILAKIQAEEKQRRLDEAKEKLAIDKEKLRLKKEALQRELEERNKAERQKkmDDEERHREKERQKKAERDARL 937
Cdd:PRK12705   51 EAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQL--EEREKALSARELELEELEKQL 128
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 392896884  938 QFAKENAAKLAAQEAKKDI--SLKSRLEQasmQQRERQKIDVQQAKLEAER 986
Cdd:PRK12705  129 DNELYRVAGLTPEQARKLLlkLLDAELEE---EKAQRVKKIEEEADLEAER 176
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
805-986 1.78e-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: 43.52  E-value: 1.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   805 IQKYRQAQVRELFEHLANQTADKGKELRKfLSSILKEIhppEDYCIKVyDPIGEE--ERKQFAILAKIQAEEKQRRLDEA 882
Cdd:TIGR02169  309 SIAEKERELEDAEERLAKLEAEIDKLLAE-IEELEREI---EEERKRR-DKLTEEyaELKEELEDLRAELEEVDKEFAET 383
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   883 KEKLAidkeKLRLKKEALQRELEE------RNKAERQKKMDDEERHREK---ERQKKAERDARLqfaKENAAKLAAQEAK 953
Cdd:TIGR02169  384 RDELK----DYREKLEKLKREINElkreldRLQEELQRLSEELADLNAAiagIEAKINELEEEK---EDKALEIKKQEWK 456
                          170       180       190
                   ....*....|....*....|....*....|...
gi 392896884   954 kdisLKSRLEQASMQQRERQKIDVQQAKLEAER 986
Cdd:TIGR02169  457 ----LEQLAADLSKYEQELYDLKEEYDRVEKEL 485
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
869-989 1.84e-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: 43.51  E-value: 1.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   869 KIQAEEKQRRLDEAKEKLA----IDKEkLRLKKEALQRELEernKAERQKKMDDEERHREKE------RQKKAERDARLQ 938
Cdd:TIGR02168  171 KERRKETERKLERTRENLDrledILNE-LERQLKSLERQAE---KAERYKELKAELRELELAllvlrlEELREELEELQE 246
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 392896884   939 FAKENA---AKLAAQEAKKDISL-KSRLEQASMQqrerQKIDVQQAKLEAERILL 989
Cdd:TIGR02168  247 ELKEAEeelEELTAELQELEEKLeELRLEVSELE----EEIEELQKELYALANEI 297
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
860-971 1.85e-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: 43.27  E-value: 1.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   860 ERKQFAILAKI-----QAEEKQRRLDEAKEKLA--------------------IDKEKL--RLKKealQRELEERNKAER 912
Cdd:pfam10174  393 ERKINVLQKKIenlqeQLRDKDKQLAGLKERVKslqtdssntdtalttleealSEKERIieRLKE---QREREDRERLEE 469
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392896884   913 QKKMDDEERHREKE----RQKKAERDARLQFAKENAAKLAAQEAKKDISLKSrLEQASMQQRE 971
Cdd:pfam10174  470 LESLKKENKDLKEKvsalQPELTEKESSLIDLKEHASSLASSGLKKDSKLKS-LEIAVEQKKE 531
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
815-986 1.90e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 1.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  815 ELFEHLANQTADKGKELRKFLSSILKEIHPPEDycikVYDPIGEEERKQFAILAKIQaeEKQRRLDEAKEKLA-IDKEKL 893
Cdd:PRK03918  158 DDYENAYKNLGEVIKEIKRRIERLEKFIKRTEN----IEELIKEKEKELEEVLREIN--EISSELPELREELEkLEKEVK 231
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  894 RLKK-----EALQRELEERNKaeRQKKMddEERHREKERQKKaERDARLQFAKENAAKLaaQEAKKDISLKSRLEQASMQ 968
Cdd:PRK03918  232 ELEElkeeiEELEKELESLEG--SKRKL--EEKIRELEERIE-ELKKEIEELEEKVKEL--KELKEKAEEYIKLSEFYEE 304
                         170
                  ....*....|....*....
gi 392896884  969 QRER-QKIDVQQAKLEAER 986
Cdd:PRK03918  305 YLDElREIEKRLSRLEEEI 323
Caldesmon pfam02029
Caldesmon;
858-936 1.90e-03

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 42.93  E-value: 1.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   858 EEERKQFaILAKIQAEEKQRRLDEAKEKlaiDKEKLRLKKEALQRELEERNKA--ERQKKMDDEERHR---EKERQKKAE 932
Cdd:pfam02029  237 EEEAEVF-LEAEQKLEELRRRRQEKESE---EFEKLRQKQQEAELELEELKKKreERRKLLEEEEQRRkqeEAERKLREE 312

                   ....
gi 392896884   933 RDAR 936
Cdd:pfam02029  313 EEKR 316
CCDC47 pfam07946
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ...
858-933 1.94e-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: 1.94e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392896884   858 EEERKQFAilaKIQAEEKQrrldeakEKLAIDKEKLRLKKEalqRELEERNKAERQKKMDdeerhrEKERQKKAER 933
Cdd:pfam07946  267 EEEIEKIK---KAAEEERA-------EEAQEKKEEAKKKER---EEKLAKLSPEEQRKYE------EKERKKEQRK 323
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
858-996 2.19e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.58  E-value: 2.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  858 EEERKQFAILAKIQAEekQRRLDEAKEKLAIDKEKLRLKKEALQRELEERNKAERQKKMDDEERHREKERQKKAERDARL 937
Cdd:COG4372   108 EEAEELQEELEELQKE--RQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQAL 185
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 392896884  938 QFAKENAAKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAERILLLSKYPNF 996
Cdd:COG4372   186 DELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALEL 244
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
874-985 2.78e-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: 2.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   874 EKQRRLDEAKEKLAIDKEKLRLKKEAL------QRELEERNKAERQKKMDDEERHR---------EKERQKKAERDARLQ 938
Cdd:TIGR02168  674 ERRREIEELEEKIEELEEKIAELEKALaelrkeLEELEEELEQLRKELEELSRQISalrkdlarlEAEVEQLEERIAQLS 753
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 392896884   939 FAKENAAKLAAQEAKKDISLKSRLEQASmQQRERQKIDVQQAKLEAE 985
Cdd:TIGR02168  754 KELTELEAEIEELEERLEEAEEELAEAE-AEIEELEAQIEQLKEELK 799
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
858-986 2.85e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 2.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  858 EEERKQFAILAKIQAEEKQRRLDEAKEKLAIDKEKLRLKKEALQRELEERNK--------------AERQKKMDDEERHR 923
Cdd:COG4717   369 EQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEEllealdeeeleeelEELEEELEELEEEL 448
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392896884  924 EKERQKKAERDARLQFAkENAAKLAAQEAKKDiSLKSRLEQASmqqRERQKIDVQQAKLEAER 986
Cdd:COG4717   449 EELREELAELEAELEQL-EEDGELAELLQELE-ELKAELRELA---EEWAALKLALELLEEAR 506
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
858-1016 2.90e-03

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


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 42.33  E-value: 2.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  858 EEERKQFAILAKIQAEEKQRRLDEAKEKLAIDKEKLRLKKEALQRELEERNKAERQKKMDDEERHREKERQKKAERDARL 937
Cdd:COG3064    92 KAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAA 171
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392896884  938 QFAKENAAKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAERILLLSKYPNFGKGPTAAAATRPQVTAKQVP 1016
Cdd:COG3064   172 ARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEE 250
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
901-987 2.96e-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: 42.42  E-value: 2.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   901 QRELEERNKAERQKKMDDEERHREKErQKKAERDARLQFAKENAAKLAAQEakKDISLKSRLEQASMQ-QRERQKIDVQQ 979
Cdd:pfam17380  281 QKAVSERQQQEKFEKMEQERLRQEKE-EKAREVERRRKLEEAEKARQAEMD--RQAAIYAEQERMAMErERELERIRQEE 357

                   ....*...
gi 392896884   980 AKLEAERI 987
Cdd:pfam17380  358 RKRELERI 365
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
812-951 3.32e-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: 42.65  E-value: 3.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   812 QVRELFEHLANQTADKgkELRKFLSSILKEIHPPEDYCIKVYDPIGEEERKQFAILAKIQAEEKQRRLDEAKEKLAIDKE 891
Cdd:TIGR00618  373 QQHTLTQHIHTLQQQK--TTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCT 450
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392896884   892 KLRLK-KEALQRELEERNKAERQKKMDDEERHrEKERQKKAERDARLQFAKENAAKLAAQE 951
Cdd:TIGR00618  451 AQCEKlEKIHLQESAQSLKEREQQLQTKEQIH-LQETRKKAVVLARLLELQEEPCPLCGSC 510
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
858-980 3.38e-03

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


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 41.75  E-value: 3.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   858 EEERKqfailAKIQAEEKQRRlDEAKEKLAIDKEKLRLKKEALQRElEERNKAERQKKmddeerHREKERQKKAERDARL 937
Cdd:TIGR02794  153 EEEAK-----AKAAAEAKKKA-EEAKKKAEAEAKAKAEAEAKAKAE-EAKAKAEAAKA------KAAAEAAAKAEAEAAA 219
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 392896884   938 QFAKEnaAKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQA 980
Cdd:TIGR02794  220 AAAAE--AERKADEAELGDIFGLASGSNAEKQGGARGAAAGSE 260
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
857-986 3.42e-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: 42.47  E-value: 3.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   857 GEEERKQFAI---LAKIQAEEKQrrldEAKEKLaiDKEKLRLKKE------ALQRELEERNKAE-RQKKMDD---EERH- 922
Cdd:pfam01576  543 LEEGKKRLQReleALTQQLEEKA----AAYDKL--EKTKNRLQQElddllvDLDHQRQLVSNLEkKQKKFDQmlaEEKAi 616
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392896884   923 --REKERQKKAERDARLQFAKenAAKLA-----AQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAER 986
Cdd:pfam01576  617 saRYAEERDRAEAEAREKETR--ALSLAraleeALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELER 685
cdk7 TIGR00570
CDK-activating kinase assembly factor MAT1; All proteins in this family for which functions ...
809-964 3.57e-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: 3.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   809 RQAQVR-ELFEhlaNQTADKGKELRKflsSILKEIHPPED--YCIKVYDPIGEE-ERKQFAILAKIQAEEKQRRLD---- 880
Cdd:TIGR00570   54 RKNNFRvQLFE---DPTVEKEVDIRK---RVLKIYNKREEdfPSLREYNDYLEEvEDIVYNLTNNIDLENTKKKIEtyqk 127
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   881 EAKEKLAIDKEKLRLKKEALQRELEERNKAERQKKMDDEERHREKERQKKAERDA---RLQFAKENAAKLAAQEAKKDIS 957
Cdd:TIGR00570  128 ENKDVIQKNKEKSTREQEELEEALEFEKEEEEQRRLLLQKEEEEQQMNKRKNKQAlldELETSTLPAAELIAQHKKNSVK 207

                   ....*..
gi 392896884   958 LKSRLEQ 964
Cdd:TIGR00570  208 LEMQVEK 214
Taxilin pfam09728
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ...
861-993 3.63e-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: 41.48  E-value: 3.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   861 RKQFAILakiQAEEKQRRLDEAKEKLAidKEKLrlkkEALQRELEERNKA---ERQKKMDDEERHR----EKERQKKAER 933
Cdd:pfam09728   45 KKKQDQL---QKEKDQLQSELSKAILA--KSKL----EKLCRELQKQNKKlkeESKKLAKEEEEKRkelsEKFQSTLKDI 115
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392896884   934 DARLQFAKENAAKLAAQE---AKKdisLKSRLEQasMQQRErQKIDVQQAKLEAERILLLSKY 993
Cdd:pfam09728  116 QDKMEEKSEKNNKLREENeelREK---LKSLIEQ--YELRE-LHFEKLLKTKELEVQLAEAKL 172
NPIP pfam06409
Nuclear pore complex interacting protein (NPIP); This family consists of a series of primate ...
860-937 3.68e-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: 41.26  E-value: 3.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   860 ERKQFAILAKIQAEEKQRRLDEAKEKLAIDKEKLRlKKEALQRELEERNK----AERQKKMDDEERHREKERQKKAERDA 935
Cdd:pfam06409   93 ERKQEAIICKLEDIFKLNRHDEIKGKAKIAKEHLR-KKSMKEDEHGEKEKqakeAEEKGKLDEKEHGEKEEMFQEAEALG 171

                   ..
gi 392896884   936 RL 937
Cdd:pfam06409  172 KL 173
PRK12704 PRK12704
phosphodiesterase; Provisional
868-989 3.97e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.07  E-value: 3.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  868 AKIQAEEKQRR--LDEAKEKL-AIDKEK-LRLKKEALQRELE-ERNKAERQKKMDD-EERHREKERQ--KKAE----RDA 935
Cdd:PRK12704   31 AKIKEAEEEAKriLEEAKKEAeAIKKEAlLEAKEEIHKLRNEfEKELRERRNELQKlEKRLLQKEENldRKLEllekREE 110
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 392896884  936 RLQFAKENAAKLaAQEAKKdisLKSRLEQASMQQRER-QKIdvqqAKL---EAERILL 989
Cdd:PRK12704  111 ELEKKEKELEQK-QQELEK---KEEELEELIEEQLQElERI----SGLtaeEAKEILL 160
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
806-984 4.07e-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: 41.80  E-value: 4.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   806 QKYRQAQVRELFEHLANQTADKGKELRKFLSSiLKEIHPPEDYCIKVYDPIGEEERKQFAILAKiQAEEKQRRLDEAKEK 885
Cdd:pfam07888   60 EKERYKRDREQWERQRRELESRVAELKEELRQ-SREKHEELEEKYKELSASSEELSEEKDALLA-QRAAHEARIRELEED 137
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   886 LAIDKEKLRLKKEALQRELEERNKAERQKKMDDEER---------------HREKERQK----KAERDARLQFAKENAAK 946
Cdd:pfam07888  138 IKTLTQRVLERETELERMKERAKKAGAQRKEEEAERkqlqaklqqteeelrSLSKEFQElrnsLAQRDTQVLQLQDTITT 217
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392896884   947 L-----------AAQEA-KKDI-SLKSRL------------EQASM-QQRERQKIDVQQAKLEA 984
Cdd:pfam07888  218 LtqklttahrkeAENEAlLEELrSLQERLnaserkveglgeELSSMaAQRDRTQAELHQARLQA 281
CCDC34 pfam13904
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ...
858-946 4.83e-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: 40.46  E-value: 4.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   858 EEERKQfaiLAKIQAEE--KQRRLDEAKEKLAIDKEKLRLK---------KEALQRELEERNKAERQKKMDDEERHREKE 926
Cdd:pfam13904   86 AELRKR---LAKEKYQEwlQRKARQQTKKREESHKQKAAESaskslakpeRKVSQEEAKEVLQEWERKKLEQQQRKREEE 162
                           90       100
                   ....*....|....*....|
gi 392896884   927 RQKKAERDARLQFAKENAAK 946
Cdd:pfam13904  163 QREQLKKEEEEQERKQLAEK 182
PRK01294 PRK01294
lipase secretion chaperone;
857-986 4.94e-03

lipase secretion chaperone;


Pssm-ID: 234937 [Multi-domain]  Cd Length: 336  Bit Score: 41.20  E-value: 4.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  857 GEEERKQFAILAKIQ--------AEEKQRRLDEAKEKLAIDkEKLRLKKEALQRELEERNKAERQKKMDDEERhrekerq 928
Cdd:PRK01294  182 GEENQYQRYALERLRiaqdpslsDAQKAARLAALEAQLPED-LRAALQESQRQQALLQQLAQLQASGASPQEL------- 253
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 392896884  929 kkaeRDARLQFAKENAAKLAAQEAKKDISLKSRLEQasmQQRERQKIDVQQAKLEAER 986
Cdd:PRK01294  254 ----RLMRAQLVGPEAAQRLEQLDQQRAAWQQRYDD---YLAQRAQILNAAGLSPQDR 304
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
873-991 5.82e-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: 40.43  E-value: 5.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   873 EEKQRRLDEAKEKLAidkeklrlKKEALQRELEERNKAERQkkmddeerhREKERQKKAErdARLQFAKENAAKLAAQEA 952
Cdd:pfam04012   32 RDMQSELVKARQALA--------QTIARQKQLERRLEQQTE---------QAKKLEEKAQ--AALTKGNEELAREALAEK 92
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 392896884   953 KKDISLKSRLEQASMQQRER--------QKIDVQQAKLEAERILLLS 991
Cdd:pfam04012   93 KSLEKQAEALETQLAQQRSAveqlrkqlAALETKIQQLKAKKNLLKA 139
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
810-986 5.89e-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: 5.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  810 QAQVRELFEHL--ANQTADKGKELRKFLSSILKEIHPPEDYcikvydpiGEEERKQFAILAKIQA-EEKQRRLDEAKEKL 886
Cdd:COG4913   616 EAELAELEEELaeAEERLEALEAELDALQERREALQRLAEY--------SWDEIDVASAEREIAElEAELERLDASSDDL 687
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  887 aidkEKLRLKKEALQRELEErNKAERQKKMDDEERHREKERQKKAERDaRLQFAKENAAKLAAQEAKKDisLKSRLEQAS 966
Cdd:COG4913   688 ----AALEEQLEELEAELEE-LEEELDELKGEIGRLEKELEQAEEELD-ELQDRLEAAEDLARLELRAL--LEERFAAAL 759
                         170       180
                  ....*....|....*....|...
gi 392896884  967 MQQRE---RQKIDVQQAKLEAER 986
Cdd:COG4913   760 GDAVErelRENLEERIDALRARL 782
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
858-992 6.29e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.04  E-value: 6.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  858 EEERKQFAILAKiQAEEKQRRLDEAKEKLAIDKEKL--------RLKK--EALQRE---LEERNKAERQKKMDDEERHRE 924
Cdd:COG4372    69 EQARSELEQLEE-ELEELNEQLQAAQAELAQAQEELeslqeeaeELQEelEELQKErqdLEQQRKQLEAQIAELQSEIAE 147
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392896884  925 KERQKKaERDARLQFAKENAAKLAAQEAKKDISLKSRLEQASMQQRERQKIDVQQAKLEAERILLLSK 992
Cdd:COG4372   148 REEELK-ELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPR 214
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
791-964 6.44e-03

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


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 40.19  E-value: 6.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  791 LESHVREMdhciywiqkyrQAQVRELFEHLANQTADKgKELRKFLSSILKEIhppEDYcikvydpigeEERKQFAI---- 866
Cdd:COG1842    28 LDQAIRDM-----------EEDLVEARQALAQVIANQ-KRLERQLEELEAEA---EKW----------EEKARLALekgr 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  867 --LA------KIQAEEKQRRLDEAKEKLAIDKEKLRLKKEALQRELEE-RNK----------AERQKKMDDE-------- 919
Cdd:COG1842    83 edLArealerKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEElKAKkdtlkarakaAKAQEKVNEAlsgidsdd 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 392896884  920 -----ERHREKERQKKAERDARLQFAKEN--AAKLAAQEAKKDISlkSRLEQ 964
Cdd:COG1842   163 atsalERMEEKIEEMEARAEAAAELAAGDslDDELAELEADSEVE--DELAA 212
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
898-989 6.78e-03

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 41.48  E-value: 6.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  898 EALQRELEeRNKAERQKKMDDEERHREKERQKKAERDARLQFAKENAAKLAAQEAKKDiSLKSRLEQASMQQRERQKIDV 977
Cdd:PRK11448  145 HALQQEVL-TLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLE-QLQEKAAETSQERKQKRKEIT 222
                          90
                  ....*....|..
gi 392896884  978 QQAkleAERILL 989
Cdd:PRK11448  223 DQA---AKRLEL 231
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
898-986 7.99e-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: 38.32  E-value: 7.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   898 EALQRELEERnKAERQKKMDDEERHREKERQKKAERDARLQ----FAKENAAKL--AAQEAKKDISLKSRLEQasmqqrE 971
Cdd:pfam13863    9 FLVQLALDAK-REEIERLEELLKQREEELEKKEQELKEDLIkfdkFLKENDAKRrrALKKAEEETKLKKEKEK------E 81
                           90
                   ....*....|....*
gi 392896884   972 RQKIDVQQAKLEAER 986
Cdd:pfam13863   82 IKKLTAQIEELKSEI 96
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
857-980 8.33e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.18  E-value: 8.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884  857 GEEERKQfAILAKIQAEEKQRRLDEAKEKLAIDKEKL-RLKK--------EALQRELEERN-KAERQKKMDDEERHREKE 926
Cdd:PRK02224  553 AEEKREA-AAEAEEEAEEAREEVAELNSKLAELKERIeSLERirtllaaiADAEDEIERLReKREALAELNDERRERLAE 631
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 392896884  927 RQkkaERDARLQFAKENAAKLAAQEAKKdiSLKSRLEQAS--MQQRERQKIDVQQA 980
Cdd:PRK02224  632 KR---ERKRELEAEFDEARIEEAREDKE--RAEEYLEQVEekLDELREERDDLQAE 682
DUF4175 pfam13779
Domain of unknown function (DUF4175);
871-988 8.90e-03

Domain of unknown function (DUF4175);


Pssm-ID: 463981 [Multi-domain]  Cd Length: 833  Bit Score: 41.13  E-value: 8.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884   871 QAEEK----QRRLDEAKEKLAIDKEKLRLK---KEALQRELEERnkAERQKKMDDEERHREKERQKKAERDA------RL 937
Cdd:pfam13779  486 DAERRlraaQERLSEALERGASDEEIAKLMqelREALDDYMQAL--AEQAQQNPQDLQQPDDPNAQEMTQQDlqrmldRI 563
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 392896884   938 QFAKENAAKLAAQEAKKDisLKSRLEQASMQQRERQKidvQQAKLEAERIL 988
Cdd:pfam13779  564 EELARSGRRAEAQQMLSQ--LQQMLENLQAGQPQQQQ---QQGQSEMQQAM 609
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
865-977 9.73e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 38.33  E-value: 9.73e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392896884    865 AILAKIQAEEKQRRlDEAKEKlaidKEKLRLKKEALQRELEERNKAERQKKmddeerhrEKERQKKAERDARLQFAKENA 944
Cdd:smart00935   18 AAQKQLEKEFKKRQ-AELEKL----EKELQKLKEKLQKDAATLSEAAREKK--------EKELQKKVQEFQRKQQKLQQD 84
                            90       100       110
                    ....*....|....*....|....*....|...
gi 392896884    945 AKLAAQEAKKDISlkSRLEQASMQQRERQKIDV 977
Cdd:smart00935   85 LQKRQQEELQKIL--DKINKAIKEVAKKKGYDL 115
 
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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