NCBI Conserved Domain Search

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

284-623

1.68e-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: 1.68e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  284 PKEPVKRKMRESESDdsviiipRKIEKEKPRPTTENVVLKKVEMEKKRPRSPELVPKKIVmEKERpsspdsEAEEREHNL 363
Cdd:COG3064    28 AAEAEQKAKEEAEEE-------RLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLA-EAEK------AAAEAEKKA 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  364 RIEKERHQKELEFRREALRKREQEREEHKKRAQEELRRQMTAALEESTRRQAEMNRQIEDEARKRDELQRIAEEKKRKQL 443
Cdd:COG3064    94 AAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAAR 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  444 LEDQCRAKQEKEKRDAEELEQMRLNIARLAGTKDVENALKSPSLVEIVPPSDARAFEMIKWNAVKCKIPENWEKRKDKFY 523
Cdd:COG3064   174 AAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAAD 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  524 RVFEWPSDAAQRDIERDEVVSIPRSKPIVIPQEDTYITRNRIPLKLPPKVKQAVPALVVRNSNNATRTVVAATVNENGIQ 603
Cdd:COG3064   254 LAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGG 333

                         330       340
                  ....*....|....*....|
gi 193205629  604 WPAETINIDEVVREIRGLMA 623
Cdd:COG3064   334 AASLEAALSLLAAGAAAAAA 353

Name

Accession

Description

Interval

E-value

ARGLU

pfam15346

Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...

322-468

7.35e-12

Pssm-ID: 405931 [Multi-domain] Cd Length: 151 Bit Score: 64.30 E-value: 7.35e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629   322 LKKVEMEKKRpRSPELVPKKIVMEKERPSspdsEAEEREHNLRIEKERHQKELEFRREALRKREQEREEHKKRAQEELRR 401
Cdd:pfam15346    5 SKLLEEETAR-RVEEAVAKRVEEELEKRK----DEIEAEVERRVEEARKIMEKQVLEELEREREAELEEERRKEEEERKK 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 193205629   402 QmtaalEESTRRQAEMNRQIEdEARKRDELQRIAEekkrkqlLEDQCRAKQEKEKRDAEELEQMRLN 468
Cdd:pfam15346   80 R-----EELERILEENNRKIE-EAQRKEAEERLAM-------LEEQRRMKEERQRREKEEEEREKRE 133

PTZ00121

MAEBL; Provisional

306-464

3.51e-11

MAEBL; Provisional

Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 67.86 E-value: 3.51e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  306 RKIEKEKPRPTTENVVLKKVEMEKKRPRSPELVPKKIVMEKERPSSPDSEAEEREhnlRIEKERHQKELEFRREALRKRE 385
Cdd:PTZ00121 1564 KKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEA---KIKAEELKKAEEEKKKVEQLKK 1640

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  386 QEREEHKK-----RAQEE--LRRQMTAALEESTRRQAEMNRQIEDEARKRDELQRIAEEKKRKQlleDQCRAKQEKEKRD 458
Cdd:PTZ00121 1641 KEAEEKKKaeelkKAEEEnkIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKA---EELKKKEAEEKKK 1717


                  ....*.
gi 193205629  459 AEELEQ 464
Cdd:PTZ00121 1718 AEELKK 1723

tolA_full

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...

296-464

2.83e-09

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

Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 59.86 E-value: 2.83e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629   296 ESDDSVIIIPRKIEKEKPRPTTEnvvlkkvemEKKRPRSPELVPKKIVMEKErpsspdsEAEERehnlRIEKERHQKELE 375
Cdd:TIGR02794   36 EIIQAVLVDPGAVAQQANRIQQQ---------KKPAAKKEQERQKKLEQQAE-------EAEKQ----RAAEQARQKELE 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629   376 FRR---EALRKREQERE--EHKKRAQEELRRQmtAALEESTRRQAEMNRQIEDEARKRDELQRIAEEKKRKQLLEDQCRA 450
Cdd:TIGR02794   96 QRAaaeKAAKQAEQAAKqaEEKQKQAEEAKAK--QAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKK 173

                          170
                   ....*....|....
gi 193205629   451 KQEKEKRDAEELEQ 464
Cdd:TIGR02794  174 KAEAEAKAKAEAEA 187

Smc

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

354-473

7.13e-09

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.95 E-value: 7.13e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  354 SEAEEREHNLRIEKERHQKELEFRREALR--KREQEREEHKKRAQEELRRQMTAALEESTRRQAEMNRQIEDEARKRDEL 431
Cdd:COG1196   263 AELEAELEELRLELEELELELEEAQAEEYelLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEEL 342

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 193205629  432 Q-RIAEEKKRKQLLEDQCRAKQEKEKRDAEELEQMRLNIARLA 473
Cdd:COG1196   343 EeELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385

ATP-synt_Fo_b

cd06503

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...

355-443

3.69e-04

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: 41.65 E-value: 3.69e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  355 EAEEREHNLRIEKERHQKELEfrrEALRKREQEREEHKKRAQEELRRQMTAALEESTRRQAEMNRQIEDEARK-----RD 429
Cdd:cd06503    41 EAEKAKEEAEELLAEYEEKLA---EARAEAQEIIEEARKEAEKIKEEILAEAKEEAERILEQAKAEIEQEKEKalaelRK 117

                          90
                  ....*....|....
gi 193205629  430 ELQRIAEEKKRKQL 443
Cdd:cd06503   118 EVADLAVEAAEKIL 131

TolA

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

284-623

1.68e-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: 1.68e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  284 PKEPVKRKMRESESDdsviiipRKIEKEKPRPTTENVVLKKVEMEKKRPRSPELVPKKIVmEKERpsspdsEAEEREHNL 363
Cdd:COG3064    28 AAEAEQKAKEEAEEE-------RLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLA-EAEK------AAAEAEKKA 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  364 RIEKERHQKELEFRREALRKREQEREEHKKRAQEELRRQMTAALEESTRRQAEMNRQIEDEARKRDELQRIAEEKKRKQL 443
Cdd:COG3064    94 AAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAAR 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  444 LEDQCRAKQEKEKRDAEELEQMRLNIARLAGTKDVENALKSPSLVEIVPPSDARAFEMIKWNAVKCKIPENWEKRKDKFY 523
Cdd:COG3064   174 AAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAAD 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  524 RVFEWPSDAAQRDIERDEVVSIPRSKPIVIPQEDTYITRNRIPLKLPPKVKQAVPALVVRNSNNATRTVVAATVNENGIQ 603
Cdd:COG3064   254 LAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGG 333

                         330       340
                  ....*....|....*....|
gi 193205629  604 WPAETINIDEVVREIRGLMA 623
Cdd:COG3064   334 AASLEAALSLLAAGAAAAAA 353

growth_prot_Scy

NF041483

polarized growth protein Scy;

354-470

2.03e-03

polarized growth protein Scy;

Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 42.12 E-value: 2.03e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  354 SEAEEREHNLRIEKErhqkelefrrEALRKREQEREEHKKRAQEELRRQMTAALEESTRRQAEMNRQIED-EARKRDELQ 432
Cdd:NF041483  509 TEAIERATTLRRQAE----------ETLERTRAEAERLRAEAEEQAEEVRAAAERAARELREETERAIAArQAEAAEELT 578

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 193205629  433 RI---AEEK--KRKQLLEDqCRAKQEKEKRDA-EELEQMRLNIA 470
Cdd:NF041483  579 RLhteAEERltAAEEALAD-ARAEAERIRREAaEETERLRTEAA 621

OmpH

smart00935

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...

353-439

4.13e-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: 38.72 E-value: 4.13e-03

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629    353 DSEAEEREHNLRIEKERHQKELEFRREALRkreQEREEHKKRAQEELRRQMTAALEESTRRQAEMNRQIEDEARKrdELQ 432
Cdd:smart00935   31 QAELEKLEKELQKLKEKLQKDAATLSEAAR---EKKEKELQKKVQEFQRKQQKLQQDLQKRQQEELQKILDKINK--AIK 105


                    ....*..
gi 193205629    433 RIAEEKK 439
Cdd:smart00935  106 EVAKKKG 112

Name

Accession

Description

Interval

E-value

ARGLU

pfam15346

Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...

322-468

7.35e-12

Pssm-ID: 405931 [Multi-domain] Cd Length: 151 Bit Score: 64.30 E-value: 7.35e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629   322 LKKVEMEKKRpRSPELVPKKIVMEKERPSspdsEAEEREHNLRIEKERHQKELEFRREALRKREQEREEHKKRAQEELRR 401
Cdd:pfam15346    5 SKLLEEETAR-RVEEAVAKRVEEELEKRK----DEIEAEVERRVEEARKIMEKQVLEELEREREAELEEERRKEEEERKK 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 193205629   402 QmtaalEESTRRQAEMNRQIEdEARKRDELQRIAEekkrkqlLEDQCRAKQEKEKRDAEELEQMRLN 468
Cdd:pfam15346   80 R-----EELERILEENNRKIE-EAQRKEAEERLAM-------LEEQRRMKEERQRREKEEEEREKRE 133

PTZ00121

MAEBL; Provisional

306-464

3.51e-11

MAEBL; Provisional

Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 67.86 E-value: 3.51e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  306 RKIEKEKPRPTTENVVLKKVEMEKKRPRSPELVPKKIVMEKERPSSPDSEAEEREhnlRIEKERHQKELEFRREALRKRE 385
Cdd:PTZ00121 1564 KKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEA---KIKAEELKKAEEEKKKVEQLKK 1640

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  386 QEREEHKK-----RAQEE--LRRQMTAALEESTRRQAEMNRQIEDEARKRDELQRIAEEKKRKQlleDQCRAKQEKEKRD 458
Cdd:PTZ00121 1641 KEAEEKKKaeelkKAEEEnkIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKA---EELKKKEAEEKKK 1717


                  ....*.
gi 193205629  459 AEELEQ 464
Cdd:PTZ00121 1718 AEELKK 1723

MAP7

pfam05672

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...

357-472

1.23e-10

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

Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 60.82 E-value: 1.23e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629   357 EEREHNLRIEKERHQKElefRREALRKREQEREEHKKRAQEELRRQmtaalEESTRRQAEMNRQIEDEARKRDELQRIAE 436
Cdd:pfam05672   17 AEKRRQAREQREREEQE---RLEKEEEERLRKEELRRRAEEERARR-----EEEARRLEEERRREEEERQRKAEEEAEER 88

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 193205629   437 EKKRKQLLEDQCRAKQEKEKRDAEELEQMRLNIARL 472
Cdd:pfam05672   89 EQREQEEQERLQKQKEEAEAKAREEAERQRQEREKI 124

DUF4670

pfam15709

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...

294-467

1.68e-10

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: 64.59 E-value: 1.68e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629   294 ESESDDSVIIIPrKIEKEKP---RPTTENVVLKKVEMEKKRprspelvpkkivMEKERPSSPDSEAEEREHNLRIEKERH 370
Cdd:pfam15709  315 RSEEDPSKALLE-KREQEKAsrdRLRAERAEMRRLEVERKR------------REQEEQRRLQQEQLERAEKMREELELE 381

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629   371 QKElefRREALRKREQEREEHKKRAQEELR---RQMTAALEESTRRQAEMNRQIEDEARKR--DELQRIAEEKKRKQLLE 445
Cdd:pfam15709  382 QQR---RFEEIRLRKQRLEEERQRQEEEERkqrLQLQAAQERARQQQEEFRRKLQELQRKKqqEEAERAEAEKQRQKELE 458

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 193205629   446 DQC---------------------------RAKQEKEKRDAEELEQMRL 467
Cdd:pfam15709  459 MQLaeeqkrlmemaeeerleyqrqkqeaeeKARLEAEERRQKEEEAARL 507

PTZ00121

MAEBL; Provisional

306-463

4.83e-10

MAEBL; Provisional

Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 64.01 E-value: 4.83e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  306 RKIEKEKPRPTTenvvLKKVEMEKKRPRSPelvpkKIVMEKERPSSPDSEAEEREHNLRIEKERHQKELEFRR-EALRKR 384
Cdd:PTZ00121 1613 KKAEEAKIKAEE----LKKAEEEKKKVEQL-----KKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKaEEAKKA 1683

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 193205629  385 EQEreehKKRAQEELRRQmtaalEESTRRQAEMNRQIEDEARKRDELQRIAEEKKRKQlleDQCRAKQEKEKRDAEELE 463
Cdd:PTZ00121 1684 EED----EKKAAEALKKE-----AEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKA---EEAKKEAEEDKKKAEEAK 1750

ATAD3_N

pfam12037

ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ...

355-470

6.89e-10

ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal domain of ATPase family AAA domain-containing protein 3 (ATAD3) which is involved in dimerization and interacts with the inner surface of the outer mitochondrial membrane. This domain is found associated with the AAA ATPase domain (pfam00004). ATAD3 is essential for mitochondrial network organization, mitochondrial metabolism and cell growth at organizm and cellular level. It may also play an important role in mitochondrial protein synthesis.

Pssm-ID: 463442 [Multi-domain] Cd Length: 264 Bit Score: 60.77 E-value: 6.89e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629   355 EAEEREHNLRIEKERHQKELEFRREALRKREQE-REEHKKRAQEELRRQmtaalEESTRRQAEMNRQIEDEARKRDELQR 433
Cdd:pfam12037   84 EYEERRKTLQEETKQKQQRAQYQDELARKRYQDqLEAQRRRNEELLRKQ-----EESVAKQEAMRIQAQRRQTEEHEAEL 158

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 193205629   434 IAEEKKRKQLLEDQCRAKQEKEKRDAeELEQMRLNIA 470
Cdd:pfam12037  159 RRETERAKAEAEAEARAKEERENEDL-NLEQLREKAN 194

tolA_full

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...

296-464

2.83e-09

Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 59.86 E-value: 2.83e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629   296 ESDDSVIIIPRKIEKEKPRPTTEnvvlkkvemEKKRPRSPELVPKKIVMEKErpsspdsEAEERehnlRIEKERHQKELE 375
Cdd:TIGR02794   36 EIIQAVLVDPGAVAQQANRIQQQ---------KKPAAKKEQERQKKLEQQAE-------EAEKQ----RAAEQARQKELE 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629   376 FRR---EALRKREQERE--EHKKRAQEELRRQmtAALEESTRRQAEMNRQIEDEARKRDELQRIAEEKKRKQLLEDQCRA 450
Cdd:TIGR02794   96 QRAaaeKAAKQAEQAAKqaEEKQKQAEEAKAK--QAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKK 173

                          170
                   ....*....|....
gi 193205629   451 KQEKEKRDAEELEQ 464
Cdd:TIGR02794  174 KAEAEAKAKAEAEA 187

DUF5401

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

308-483

3.47e-09

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: 60.91 E-value: 3.47e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629   308 IEKEKPRPTTEnvvlKKVEMEKKRPRSPELVPKKI-VMEKERPSSPD---SEAEEREHNLRI----EKERHQKELEFRRE 379
Cdd:pfam17380  407 LEEERQRKIQQ----QKVEMEQIRAEQEEARQREVrRLEEERAREMErvrLEEQERQQQVERlrqqEEERKRKKLELEKE 482

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629   380 AlRKREQEREEHKKRAQEELRRQMTAALEESTRRQAeMNRQIED--EARKRDELQRIAEEKKRKQLLEDQCRAKQEKEKR 457
Cdd:pfam17380  483 K-RDRKRAEEQRRKILEKELEERKQAMIEEERKRKL-LEKEMEErqKAIYEEERRREAEEERRKQQEMEERRRIQEQMRK 560

                          170       180
                   ....*....|....*....|....*....
gi 193205629   458 DAEE---LEQMRLNIARLAGTKDVENALK 483
Cdd:pfam17380  561 ATEErsrLEAMEREREMMRQIVESEKARA 589

DUF4670

pfam15709

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...

327-473

3.93e-09

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: 60.35 E-value: 3.93e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629   327 MEKKRPRSPELvPKKIVMEK--ERPSSPDSEAEEREHNLRIEKERHQKElefrREALRKREQEREEHKKRAQEELRRQMT 404
Cdd:pfam15709  309 MESEEERSEED-PSKALLEKreQEKASRDRLRAERAEMRRLEVERKRRE----QEEQRRLQQEQLERAEKMREELELEQQ 383

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629   405 AALEE----STRRQAEMNRQIEDEARKRDELQ------RIAEEKKRKQLLEDQCRAKQEK-EKRDAEELEQMRLNIaRLA 473
Cdd:pfam15709  384 RRFEEirlrKQRLEEERQRQEEEERKQRLQLQaaqeraRQQQEEFRRKLQELQRKKQQEEaERAEAEKQRQKELEM-QLA 462

Smc

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

354-473

7.13e-09

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.95 E-value: 7.13e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  354 SEAEEREHNLRIEKERHQKELEFRREALR--KREQEREEHKKRAQEELRRQMTAALEESTRRQAEMNRQIEDEARKRDEL 431
Cdd:COG1196   263 AELEAELEELRLELEELELELEEAQAEEYelLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEEL 342

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 193205629  432 Q-RIAEEKKRKQLLEDQCRAKQEKEKRDAEELEQMRLNIARLA 473
Cdd:COG1196   343 EeELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385

PTZ00121

MAEBL; Provisional

286-464

7.23e-09

MAEBL; Provisional

Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.15 E-value: 7.23e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  286 EPVKRKMRESESDDSVIIIPRKIEKEKPRPTTENVVLKKVEMEKKRPRSPELvpKKIVMEKERPSSPDSEAEE---REHN 362
Cdd:PTZ00121 1332 DAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAA--KKKAEEKKKADEAKKKAEEdkkKADE 1409

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  363 LRIEKERHQKELEFRREALRKREQEreEHKKRAqEELRRQMTAALEESTRRQAEMNRQIEDEARKRDELQRIAEEKKRKq 442
Cdd:PTZ00121 1410 LKKAAAAKKKADEAKKKAEEKKKAD--EAKKKA-EEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKA- 1485

                         170       180
                  ....*....|....*....|..
gi 193205629  443 lleDQCRAKQEKEKRDAEELEQ 464
Cdd:PTZ00121 1486 ---DEAKKKAEEAKKKADEAKK 1504

Smc

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

355-473

1.38e-08

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.18 E-value: 1.38e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  355 EAEEREHNLRIEKERHQKELEFRREALRKREQEREEHKKRAQEELRRQMT---AALEESTRRQAEMNRQIEDEARKRDEL 431
Cdd:COG1196   334 ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEElaeELLEALRAAAELAAQLEELEEAEEALL 413

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 193205629  432 QRIAEEKKRKQLLEDQCRAKQEKEKRDAEELEQMRLNIARLA 473
Cdd:COG1196   414 ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE 455

DUF5401

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

291-461

1.84e-08

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: 58.60 E-value: 1.84e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629   291 KMRESESddsvIIIPRKIEKEKPRPTTENVVLKKVeMEKKRPRspELVPKKIVMEKERPSspdsEAEEREHNLRIEKERH 370
Cdd:pfam17380  376 RMRELER----LQMERQQKNERVRQELEAARKVKI-LEEERQR--KIQQQKVEMEQIRAE----QEEARQREVRRLEEER 444

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629   371 QKELEFRREALRKREQEREEHKKRAQEELRRQMTAALEESTRRQAEMNRQIEDEARKRDELQRIAEEKKRKQLLEDQCRA 450
Cdd:pfam17380  445 AREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEE 524

                          170
                   ....*....|....*.
gi 193205629   451 KQ-----EKEKRDAEE 461
Cdd:pfam17380  525 RQkaiyeEERRREAEE 540

PTZ00121

MAEBL; Provisional

276-462

2.48e-08

MAEBL; Provisional

Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.61 E-value: 2.48e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  276 RSIRPPETPKEPVKRKMRESESDDSVIIIPRKIEKEKPRPTTENVVLKKVEMEKKRPRSPELVPKKIVMEKERPSSPDSE 355
Cdd:PTZ00121 1593 RIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEE 1672

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  356 AEEREHNLRIEKERHQKelefRREALRKREQER---EEHKKRAQEELRR--QMTAALEESTRRQAEMNRQIEDEARKRDE 430
Cdd:PTZ00121 1673 DKKKAEEAKKAEEDEKK----AAEALKKEAEEAkkaEELKKKEAEEKKKaeELKKAEEENKIKAEEAKKEAEEDKKKAEE 1748

                         170       180       190
                  ....*....|....*....|....*....|..
gi 193205629  431 LQRIAEEKKRKQLLEDQCRAKQEKEKRDAEEL 462
Cdd:PTZ00121 1749 AKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAV 1780

Smc

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

355-473

3.41e-08

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.64 E-value: 3.41e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  355 EAEEREHNLRIEK-ERHQKELEFRREALRKREQEREEHKKRAQEELRRQMTAALEESTRRQAEMNRQIEDEARKRDELQR 433
Cdd:COG1196   245 EAELEELEAELEElEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEE 324

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 193205629  434 IAEEKKRKQLLEDQCRAKQEKEKRDAEELEQMRLNIARLA 473
Cdd:COG1196   325 LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364

Smc

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

354-473

4.28e-08

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.25 E-value: 4.28e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  354 SEAEEREHNLRI-EKERHQKELEFRREALRKREQEREEHKKRAQ------EELRRQMTAALEESTRRQAEMN----RQIE 422
Cdd:COG1196   220 EELKELEAELLLlKLRELEAELEELEAELEELEAELEELEAELAeleaelEELRLELEELELELEEAQAEEYellaELAR 299

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 193205629  423 DEARKRDELQRIAEEKKRKQLLEDQCRAKQEKEKRDAEELEQMRLNIARLA 473
Cdd:COG1196   300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE 350

Smc

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

355-481

4.32e-08

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.25 E-value: 4.32e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  355 EAEEREHNLRIEKERHQKELEFRREALRKREQEREEHKKRAQEELRRQMTAALEESTRRQAEMNRQIEDEARKRDELQRI 434
Cdd:COG1196   302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 193205629  435 AEEKKRKQLLEDQCRAKQEKEKRDAEELEQMRLNIARLAGTKDVENA 481
Cdd:COG1196   382 EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428

PTZ00121

MAEBL; Provisional

323-464

4.68e-08

MAEBL; Provisional

Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.46 E-value: 4.68e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  323 KKVEMEKKRprSPELvpKKIVMEKERPSSPDSEAEER----EHNLRIEKERHQKELEFRREALRKREQ--EREEHKKRAQ 396
Cdd:PTZ00121 1398 KKAEEDKKK--ADEL--KKAAAAKKKADEAKKKAEEKkkadEAKKKAEEAKKADEAKKKAEEAKKAEEakKKAEEAKKAD 1473

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 193205629  397 EELRRQMTAALEESTRRQAEMNRQIEDEARKRDELQRIAEEKKRKQLLEDQCRAKQEKEKRDAEELEQ 464
Cdd:PTZ00121 1474 EAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKK 1541

Smc

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

355-481

7.90e-08

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.48 E-value: 7.90e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  355 EAEEREHNLRIEKERHQKELEFRREALRKREQEREEhkkrAQEELRRQMTAALEESTRRQAEMNRQIEDEARKRDELQRI 434
Cdd:COG1196   320 ELEEELAELEEELEELEEELEELEEELEEAEEELEE----AEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 193205629  435 AEEKKRKQLLEDQCRAKQEKEKRDAEELEQMRLNIARLAGTKDVENA 481
Cdd:COG1196   396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE 442

Smc

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

355-473

1.28e-07

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.71 E-value: 1.28e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  355 EAEEREHNLRIEKERHQKELEFRREALRKREQEREEHKKRAQEELRRQMTAALEESTRRQAEMN---RQIEDEARKRDEL 431
Cdd:COG1196   327 ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEalrAAAELAAQLEELE 406

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 193205629  432 QRIAEEKKRKQLLEDQCRAKQEKEKRDAEELEQMRLNIARLA 473
Cdd:COG1196   407 EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448

Smc

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

355-473

1.42e-07

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.71 E-value: 1.42e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  355 EAEEREHNLRIEKERHQKELEFRREALR------KREQEREEHKKRAQEELRRQMTAALEESTRRQAEMNRQIEDEARKR 428
Cdd:COG1196   285 EAQAEEYELLAELARLEQDIARLEERRReleerlEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 193205629  429 DELQRIAEEKKRKQLLEDQCRAKQEKEKRDAEELEQMRLNIARLA 473
Cdd:COG1196   365 EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409

PTZ00121

MAEBL; Provisional

286-464

1.75e-07

MAEBL; Provisional

Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.53 E-value: 1.75e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  286 EPVKRKMRESESDDSviiIPRKIEKEKPRPTTenvvLKKVEMEKKRP---RSPELVPKKIVMEKERPSSPDSEAEEREHN 362
Cdd:PTZ00121 1473 DEAKKKAEEAKKADE---AKKKAEEAKKKADE----AKKAAEAKKKAdeaKKAEEAKKADEAKKAEEAKKADEAKKAEEK 1545

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  363 LRIEKERHQKEL----EFRREALRKREQEREEHKKRAQEELRR-------QMTAALEESTRRQAEMNRQIEDEARKRDEL 431
Cdd:PTZ00121 1546 KKADELKKAEELkkaeEKKKAEEAKKAEEDKNMALRKAEEAKKaeearieEVMKLYEEEKKMKAEEAKKAEEAKIKAEEL 1625

                         170       180       190
                  ....*....|....*....|....*....|...
gi 193205629  432 QRIAEEKKRKQlledQCRAKQEKEKRDAEELEQ 464
Cdd:PTZ00121 1626 KKAEEEKKKVE----QLKKKEAEEKKKAEELKK 1654

Smc

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

355-473

2.21e-07

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.94 E-value: 2.21e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  355 EAEEREHNLRIEKERHQ-KELEFRREALRKREQEREEHKKRAQEELRRQmTAALEESTRRQAEMNRQIEDEARKRDEL-Q 432
Cdd:COG1196   259 EAELAELEAELEELRLElEELELELEEAQAEEYELLAELARLEQDIARL-EERRRELEERLEELEEELAELEEELEELeE 337

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 193205629  433 RIAEEKKRKQLLEDQCRAKQEKEKRDAEELEQMRLNIARLA 473
Cdd:COG1196   338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378

tolA

cell envelope integrity inner membrane protein TolA; Provisional

345-461

2.53e-07

cell envelope integrity inner membrane protein TolA; Provisional

Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 54.04 E-value: 2.53e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  345 EKERPSSPDSEAEEREHNLRIEKERhQKELEFRREALRKREQEREEHKKRAQEElrrQMTAalEESTRRQAEMNRQIEDE 424
Cdd:PRK09510   78 EEQRKKKEQQQAEELQQKQAAEQER-LKQLEKERLAAQEQKKQAEEAAKQAALK---QKQA--EEAAAKAAAAAKAKAEA 151

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 193205629  425 ARKR--DELQRIAEEKKRKQLLEDQCRAKQEKEKRDAEE 461
Cdd:PRK09510  152 EAKRaaAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAE 190

PTZ00121

MAEBL; Provisional

286-464

2.65e-07

MAEBL; Provisional

Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.15 E-value: 2.65e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  286 EPVKRKMRESESDDSviiIPRKIEKEKPRPTTenvvLKKVEMEKKRprSPELvpKKIVMEKERPSSPDSEAEEREHNLRI 365
Cdd:PTZ00121 1381 DAAKKKAEEKKKADE---AKKKAEEDKKKADE----LKKAAAAKKK--ADEA--KKKAEEKKKADEAKKKAEEAKKADEA 1449

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  366 EKERHQKElefRREALRKREQER---EEHKKRAQEELRRQMTAALEESTRRQAEMNRQIEDEARKRDELQRIAEEKKRKQ 442
Cdd:PTZ00121 1450 KKKAEEAK---KAEEAKKKAEEAkkaDEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADE 1526

                         170       180
                  ....*....|....*....|....*..
gi 193205629  443 LLEDQCRAKQEK-----EKRDAEELEQ 464
Cdd:PTZ00121 1527 AKKAEEAKKADEakkaeEKKKADELKK 1553

PTZ00121

MAEBL; Provisional

279-521

3.13e-07

MAEBL; Provisional

Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.76 E-value: 3.13e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  279 RPPETPKEPVKRKMRESESDDSViiipRKIEKEKPRPTTENV-VLKKVEMEKKRPRSPELVPKKIVMEKERPSSPDSEAE 357
Cdd:PTZ00121 1189 KAEELRKAEDARKAEAARKAEEE----RKAEEARKAEDAKKAeAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAH 1264

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  358 EREHNLRIEKERHQKELEFRR-EALRKREQEREEHKKRAQEELRRQMTAALE-ESTRRQAEMNRQIEDEARKRDELQRIA 435
Cdd:PTZ00121 1265 FARRQAAIKAEEARKADELKKaEEKKKADEAKKAEEKKKADEAKKKAEEAKKaDEAKKKAEEAKKKADAAKKKAEEAKKA 1344

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  436 EEKKRKQLLEDQCRAKQEKEKRDAEELEQMRLNIARLAGTKDVENALKSPSLVEIVPPSDARAFEMIKWNAVKCKIPENW 515
Cdd:PTZ00121 1345 AEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAK 1424


                  ....*.
gi 193205629  516 EKRKDK 521
Cdd:PTZ00121 1425 KKAEEK 1430

CCDC34

pfam13904

Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ...

367-485

3.53e-07

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: 52.01 E-value: 3.53e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629   367 KERHQKELEFRREALRKREQEREEHKKRAQEEL-------RRQMTAALEESTRRQAEMNRQIEDEARKRDELQRIAEEK- 438
Cdd:pfam13904   65 QRQRQKELQAQKEEREKEEQEAELRKRLAKEKYqewlqrkARQQTKKREESHKQKAAESASKSLAKPERKVSQEEAKEVl 144

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 193205629   439 ----KRKQLLEDQCRAKQEKEKRDAEELEQMRLNIARLAGTKDVENALKSP 485
Cdd:pfam13904  145 qeweRKKLEQQQRKREEEQREQLKKEEEEQERKQLAEKAWQKWMKNVKNKP 195

Caldesmon

pfam02029

Caldesmon;

281-465

3.82e-07

Caldesmon;

Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 53.72 E-value: 3.82e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629   281 PETPKEPVKRKMRESESDDsviiiprKIEKEKPRPTTENVVL--KKVEMEKKRPRSPELVPKKIVMEKERPSSPDSEAEE 358
Cdd:pfam02029  164 EEAEEVPTENFAKEEVKDE-------KIKKEKKVKYESKVFLdqKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQER 236

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629   359 REhnlrieKERHQKELEFRREALRKREQEREEhkkRAQEELR-RQMTAA--LEESTRRQAEMNRQIEDEARKRDElqriA 435
Cdd:pfam02029  237 EE------EAEVFLEAEQKLEELRRRRQEKES---EEFEKLRqKQQEAEleLEELKKKREERRKLLEEEEQRRKQ----E 303

                          170       180       190
                   ....*....|....*....|....*....|
gi 193205629   436 EEKKRKQLLEDQCRAKQEKEKRDAEELEQM 465
Cdd:pfam02029  304 EAERKLREEEEKRRMKEEIERRRAEAAEKR 333

TPH

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...

357-467

3.84e-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: 3.84e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629   357 EEREHNLRIEKERHQKELEFRREALRK---REQEREEHKKRAQEELRRQMTAALEESTR-------RQAEMNRQIEDEAR 426
Cdd:pfam13868   83 EEREQKRQEEYEEKLQEREQMDEIVERiqeEDQAEAEEKLEKQRQLREEIDEFNEEQAEwkelekeEEREEDERILEYLK 162

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 193205629   427 KRDELQRIAEEKKR-----KQLLEDQCRAKQEKEKRDAEELEQMRL 467
Cdd:pfam13868  163 EKAEREEEREAEREeieeeKEREIARLRAQQEKAQDEKAERDELRA 208

PTZ00121

MAEBL; Provisional

309-464

4.36e-07

MAEBL; Provisional

Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.38 E-value: 4.36e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  309 EKEKPRPTTENVVLKKVEMEKKRP---RSPELVPKKIVMEKERPSSPDSEAEEREHNLRIEK---ERHQKELEFRREALR 382
Cdd:PTZ00121 1288 EKKKADEAKKAEEKKKADEAKKKAeeaKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKaeaEAAADEAEAAEEKAE 1367

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  383 KREQEREEHKKRAQ------EELRRQMTAALE-ESTRRQAEMNRQIEDEARKRDELQRIAEEKKRKQLLEdqcraKQEKE 455
Cdd:PTZ00121 1368 AAEKKKEEAKKKADaakkkaEEKKKADEAKKKaEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAK-----KKAEE 1442


                  ....*....
gi 193205629  456 KRDAEELEQ 464
Cdd:PTZ00121 1443 AKKADEAKK 1451

DUF4670

pfam15709

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...

288-461

8.27e-07

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: 8.27e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629   288 VKRKMRESESDdsviiipRKIEKEKPRptTENVVLKKVEMEKKRpRSPELVPKKIVMEKERPSSPDSEAEEREHnLRIEK 367
Cdd:pfam15709  350 VERKRREQEEQ-------RRLQQEQLE--RAEKMREELELEQQR-RFEEIRLRKQRLEEERQRQEEEERKQRLQ-LQAAQ 418

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629   368 ER-HQKELEFRREALRKREQEREEHKKRAQEELRRQ--MTAALEESTRRQAEMnrqiEDEARKRDELQRIAEEKKRKQLL 444
Cdd:pfam15709  419 ERaRQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQkeLEMQLAEEQKRLMEM----AEEERLEYQRQKQEAEEKARLEA 494

                          170
                   ....*....|....*..
gi 193205629   445 EDQcRAKQEKEKRDAEE 461
Cdd:pfam15709  495 EER-RQKEEEAARLALE 510

Smc

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

354-473

1.13e-06

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.63 E-value: 1.13e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  354 SEAEEREHNLRIEKERHQKELEFRREALRKREQEREEHKKRAQEELRRQMTAALEESTRRQAEMNRQIEDEARKRDELQR 433
Cdd:COG1196   295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 193205629  434 IAEEKKRKQLLED--QCRAKQEKEKRDAEELEQMRLNIARLA 473
Cdd:COG1196   375 AEAEEELEELAEEllEALRAAAELAAQLEELEEAEEALLERL 416

DUF5401

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

307-469

1.31e-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: 52.43 E-value: 1.31e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629   307 KIEKEKPRPTTENvvlKKVEMEKKRPRSPELVPKKIVMEKERPSSPDSE--AEEREHNL-RIEKERHQKELE-FRREAL- 381
Cdd:pfam17380  295 KMEQERLRQEKEE---KAREVERRRKLEEAEKARQAEMDRQAAIYAEQErmAMERERELeRIRQEERKRELErIRQEEIa 371

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629   382 ----RKREQER-EEHKKRAQEELRRQMTAA-----LEESTRR-------QAEMNRQIEDEARKRdELQRIAEEKKR---- 440
Cdd:pfam17380  372 meisRMRELERlQMERQQKNERVRQELEAArkvkiLEEERQRkiqqqkvEMEQIRAEQEEARQR-EVRRLEEERARemer 450

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 193205629   441 ---------------KQLLEDQCRAK--QEKEKRDAEELEQMRLNI 469
Cdd:pfam17380  451 vrleeqerqqqverlRQQEEERKRKKleLEKEKRDRKRAEEQRRKI 496

PTZ00121

MAEBL; Provisional

286-527

1.36e-06

MAEBL; Provisional

Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.84 E-value: 1.36e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  286 EPVKRKMRESESDDSViiiprKIEKEKPRPTTEnvvLKKVEMEKKRprSPELvpKKIVMEKERPSSPDSEAEER----EH 361
Cdd:PTZ00121 1408 DELKKAAAAKKKADEA-----KKKAEEKKKADE---AKKKAEEAKK--ADEA--KKKAEEAKKAEEAKKKAEEAkkadEA 1475

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  362 NLRIEKERHQKELEFRREALRKREQE---REEHKKRAQE----ELRRQMTAALEESTRRQAEMNRQIEdEARKRDELQRI 434
Cdd:PTZ00121 1476 KKKAEEAKKADEAKKKAEEAKKKADEakkAAEAKKKADEakkaEEAKKADEAKKAEEAKKADEAKKAE-EKKKADELKKA 1554

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  435 AEEKKRKQLledqcraKQEKEKRDAEELEQM---RLNIARLAGTKDVENALKSPSLVEIVPPSDARAFEMIKWNAVKCKI 511
Cdd:PTZ00121 1555 EELKKAEEK-------KKAEEAKKAEEDKNMalrKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK 1627

                         250
                  ....*....|....*.
gi 193205629  512 PENWEKRKDKFYRVFE 527
Cdd:PTZ00121 1628 AEEEKKKVEQLKKKEA 1643

Myosin_tail_1

pfam01576

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...

350-484

1.41e-06

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: 52.48 E-value: 1.41e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629   350 SSPDSEAEEREHNLRIEKERHQKELEFRREALRKREQEREEhkkraQEELRRQMTAALEESTRRQAEMNRQIED----EA 425
Cdd:pfam01576  165 TSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQE-----LEKAKRKLEGESTDLQEQIAELQAQIAElraqLA 239

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629   426 RKRDELQ----RIAEEKKRK---------------QLLED-----QCRAKQEKEKRD-AEELEQMRLNIARLAGTKDVEN 480
Cdd:pfam01576  240 KKEEELQaalaRLEEETAQKnnalkkireleaqisELQEDleserAARNKAEKQRRDlGEELEALKTELEDTLDTTAAQQ 319


                   ....
gi 193205629   481 ALKS 484
Cdd:pfam01576  320 ELRS 323

tolA

cell envelope integrity inner membrane protein TolA; Provisional

339-461

1.78e-06

cell envelope integrity inner membrane protein TolA; Provisional

Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 51.35 E-value: 1.78e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  339 PKKIVMEKERPSSPDSEAEEREHNLRIEKERHQKELEFRREALRKREQEREEHKKRAQEELRRQmtaalEESTRRQAEMN 418
Cdd:PRK09510   57 PGAVVEQYNRQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQA-----EEAAKQAALKQ 131

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 193205629  419 RQIEDEARKRDELQRIAEEKKRKQLLEDQCRAKQEKEKRDAEE 461
Cdd:PRK09510  132 KQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAE 174

TPH

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...

355-473

2.09e-06

Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 51.07 E-value: 2.09e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629   355 EAEEREHNLRIEKERHQKELEFRREALRKREQEREEHKKRAQEELRRQMTAALEESTRRQAEMNRQIEDEARKRDELQRI 434
Cdd:pfam13868   30 EKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVER 109

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 193205629   435 AEE----------KKRKQLLEDQCRAKQEKEKRDAEELEQMRLNIARLA 473
Cdd:pfam13868  110 IQEedqaeaeeklEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERIL 158

Smc

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

355-473

2.13e-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: 2.13e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  355 EAEEREHNLRIEKERHQKELEFRREALRKREQEREEHKKRAQEELRRQMTAALEESTRRQAEMNRQIEDEARKRDELQRI 434
Cdd:COG1196   379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE 458

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 193205629  435 AEEKKRKQLLEDQCRAKQEKEKRDAEELEQMRLNIARLA 473
Cdd:COG1196   459 EALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497

PTZ00121

MAEBL; Provisional

326-483

2.38e-06

MAEBL; Provisional

Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.07 E-value: 2.38e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  326 EMEKKRPRSPE--LVPKKIVMEKERPSSPDSEAEE--REHNLRIEKERHQKELEFRREALRKREQEREEHKKRAQEELRR 401
Cdd:PTZ00121 1068 QDEGLKPSYKDfdFDAKEDNRADEATEEAFGKAEEakKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARK 1147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  402 QMTAALEESTR-----RQAEMNRQIED-----EARKRDELQRIAEEKKRKQL--LEDQCRAKQEKEKRDAEELEQMRlni 469
Cdd:PTZ00121 1148 AEDAKRVEIARkaedaRKAEEARKAEDakkaeAARKAEEVRKAEELRKAEDArkAEAARKAEEERKAEEARKAEDAK--- 1224

                         170
                  ....*....|....
gi 193205629  470 aRLAGTKDVENALK 483
Cdd:PTZ00121 1225 -KAEAVKKAEEAKK 1237

TPH

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...

354-466

3.81e-06

Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 50.30 E-value: 3.81e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629   354 SEAEEREHNLRIEKERHQKELEFRREALRKrEQEREEHKKRAQEELRRQmtAALEESTRRQAEmnRQIEDEARKRDELQR 433
Cdd:pfam13868  162 KEKAEREEEREAEREEIEEEKEREIARLRA-QQEKAQDEKAERDELRAK--LYQEEQERKERQ--KEREEAEKKARQRQE 236

                           90       100       110
                   ....*....|....*....|....*....|...
gi 193205629   434 IAEEkkRKQLLEDQCRAKQEKEKRDAEELEQMR 466
Cdd:pfam13868  237 LQQA--REEQIELKERRLAEEAEREEEEFERML 267

SMC_prok_B

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...

356-481

3.97e-06

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

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.21 E-value: 3.97e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629   356 AEEREHNLRI---EKERHQKELEFRREALRKREQEREEHKKRAQ------EELRRQMTAALEESTRRQAEMNRQIEDEAR 426
Cdd:TIGR02168  220 AELRELELALlvlRLEELREELEELQEELKEAEEELEELTAELQeleeklEELRLEVSELEEEIEELQKELYALANEISR 299

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 193205629   427 KRDELQRIAEEKKR----KQLLEDQCRAKQEKEKRDAEELEQMRLNIARLAGTKDVENA 481
Cdd:TIGR02168  300 LEQQKQILRERLANlerqLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEA 358

ERM_helical

pfam20492

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...

373-464

4.24e-06

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: 46.84 E-value: 4.24e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629   373 ELEFRREALRKREQEREEHKKRAQEELRRQMTAALE-ESTRRQAEMNRQIEDEARK-----RDELQRIAE-EKKRKQLLE 445
Cdd:pfam20492    3 EAEREKQELEERLKQYEEETKKAQEELEESEETAEElEEERRQAEEEAERLEQKRQeaeeeKERLEESAEmEAEEKEQLE 82

                           90
                   ....*....|....*....
gi 193205629   446 DQCRAKQEKEKRDAEELEQ 464
Cdd:pfam20492   83 AELAEAQEEIARLEEEVER 101

Smc

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

354-473

4.35e-06

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: 4.35e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  354 SEAEEREHNLRIEKERHQKELEFRREALRKREQEREEHKKRAQEEL--RRQMTAALEESTRRQAEMNRQIEDEARKRDEL 431
Cdd:COG1196   382 EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEeaLAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 193205629  432 QRIAEEKKRKQLLEDQCRAKQEKEKRDAEELEQMRLNIARLA 473
Cdd:COG1196   462 LELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503

Smc

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

355-483

4.90e-06

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: 4.90e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  355 EAEEREHNLRIEKERHQKELEfRREALRKREQEREEHKKRAQEELRRQMTAALEESTRRQAEMNRQIEDEARKRDELQRI 434
Cdd:COG1196   278 ELELELEEAQAEEYELLAELA-RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 193205629  435 AEE--KKRKQLLEDQCRAKQEKEKRDAEELEQMRLNIARLAGTKDVENALK 483
Cdd:COG1196   357 EAElaEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE 407

PTZ00121

MAEBL; Provisional

291-484

5.09e-06

MAEBL; Provisional

Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 5.09e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  291 KMRESESDDSVIIIPRKIEKEKPRPTTENVVLKKVEMEKKRP---RSPELVPKKIVMEKERPSSPDSEAEEREHNLRIEK 367
Cdd:PTZ00121 1083 AKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAedaRKAEEARKAEDARKAEEARKAEDAKRVEIARKAED 1162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  368 ERHQKELEFRREALRKREQEREEHKKRAqEELRRQMTAALEESTRRqAEMNRQIEdEARKRDELQRIAEEKKRKQLLEDQ 447
Cdd:PTZ00121 1163 ARKAEEARKAEDAKKAEAARKAEEVRKA-EELRKAEDARKAEAARK-AEEERKAE-EARKAEDAKKAEAVKKAEEAKKDA 1239

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 193205629  448 CRAKQEKEKRDAEELEqmRLNIARLAGTKDVENALKS 484
Cdd:PTZ00121 1240 EEAKKAEEERNNEEIR--KFEEARMAHFARRQAAIKA 1274

TPH

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...

357-471

5.92e-06

Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 49.53 E-value: 5.92e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629   357 EEREHNLRIEKerHQKELEFRREALRKREQEREEHKKRAQEELRRQMTAALEE-STRRQAEMNRQIEDEARKRDELQRIA 435
Cdd:pfam13868  149 EEREEDERILE--YLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEkAERDELRAKLYQEEQERKERQKEREE 226

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 193205629   436 EEKKRKQLLE------DQCRAKQEKEKRDAEELEQMRLNIAR 471
Cdd:pfam13868  227 AEKKARQRQElqqareEQIELKERRLAEEAEREEEEFERMLR 268

PTZ00121

MAEBL; Provisional

322-556

6.19e-06

MAEBL; Provisional

Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.52 E-value: 6.19e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  322 LKKVEMEKKRPRSPELVPKKIVMEKERPSSPDSEAEEREHNLRIEKERHQKELEFRREALRKREQERE---EHKKRAQEE 398
Cdd:PTZ00121 1539 AKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKmkaEEAKKAEEA 1618

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  399 LRRQMTAALEESTRRQAE-MNRQIEDEARKRDELQRIAEEKKRKQlleDQCRAKQEKEKRDAEEL--EQMRLNIARLAGT 475
Cdd:PTZ00121 1619 KIKAEELKKAEEEKKKVEqLKKKEAEEKKKAEELKKAEEENKIKA---AEEAKKAEEDKKKAEEAkkAEEDEKKAAEALK 1695

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  476 KDVENALKSPSLVEIVPPSDARAFEMIK------WNAVKCKIPENWEKRKDKFYRVFEWPSDAAQ--RDIERDEVVSIPR 547
Cdd:PTZ00121 1696 KEAEEAKKAEELKKKEAEEKKKAEELKKaeeenkIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAhlKKEEEKKAEEIRK 1775


                  ....*....
gi 193205629  548 SKPIVIPQE 556
Cdd:PTZ00121 1776 EKEAVIEEE 1784

tolA

cell envelope integrity inner membrane protein TolA; Provisional

326-464

6.34e-06

cell envelope integrity inner membrane protein TolA; Provisional

Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 49.80 E-value: 6.34e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  326 EMEKKRPRSPELVPKKIVMEKERPSSPDSEAEEREHNLRIEKERHQKElefRREALRKREQEREEhKKRAQEELRRQMTA 405
Cdd:PRK09510   69 QQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQ---KKQAEEAAKQAALK-QKQAEEAAAKAAAA 144

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 193205629  406 A---LEESTRRQAEMNRQIEDEARKRDELQ---RIAEEKKRKQLLEDQCRAKQEKEKRDAEELEQ 464
Cdd:PRK09510  145 AkakAEAEAKRAAAAAKKAAAEAKKKAEAEaakKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKK 209

Caldesmon

pfam02029

Caldesmon;

279-499

7.34e-06

Caldesmon;

Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 49.87 E-value: 7.34e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629   279 RPPETPKEPVKRKMRESESDdsviiIPRKIEKEKPRPTTENVVLKKVEMEKKrprsPELVPKKIVMEKERPSSPDSEAEE 358
Cdd:pfam02029  143 NKWSTEVRQAEEEGEEEEDK-----SEEAEEVPTENFAKEEVKDEKIKKEKK----VKYESKVFLDQKRGHPEVKSQNGE 213

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629   359 REHNLRIEKERHQKELEFRREALRKREQEREEHKKRAqEELRRQmtaaLEESTRRQAEMNRQIEDEARKR-DELQRIAEE 437
Cdd:pfam02029  214 EEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQKL-EELRRR----RQEKESEEFEKLRQKQQEAELElEELKKKREE 288

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 193205629   438 KKRKQLLEDQCRAKQEKEKRDAEELE--QMRLNIARlagtKDVENALKSPSLVEIVPPSDARAF 499
Cdd:pfam02029  289 RRKLLEEEEQRRKQEEAERKLREEEEkrRMKEEIER----RRAEAAEKRQKLPEDSSSEGKKPF 348

PRK12704

phosphodiesterase; Provisional

355-502

7.39e-06

phosphodiesterase; Provisional

Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 49.78 E-value: 7.39e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  355 EAEEREHNLR--IEKERHQKELEFRReaLRKREQEREEHKKRAQEEL---RRQMTAALEESTRRQAEMNRQIED----EA 425
Cdd:PRK12704   61 EAKEEIHKLRneFEKELRERRNELQK--LEKRLLQKEENLDRKLELLekrEEELEKKEKELEQKQQELEKKEEEleelIE 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  426 RKRDELQRIA---EEKKRKQLLED-QCRAKQEKEKR------DAEELEQMRLN------IARLAGTKDVENALkspSLVE 489
Cdd:PRK12704  139 EQLQELERISgltAEEAKEILLEKvEEEARHEAAVLikeieeEAKEEADKKAKeilaqaIQRCAADHVAETTV---SVVN 215

                         170       180
                  ....*....|....*....|....*.
gi 193205629  490 IvpPSDA-------------RAFEMI 502
Cdd:PRK12704  216 L--PNDEmkgriigregrniRALETL 239

YqiK

COG2268

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

355-479

7.70e-06

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

Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 49.49 E-value: 7.70e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  355 EAEEREHNLRIEKErhQKELEFRREALRkREQEREehKKRAQEelrrqmtAALEESTRRQAEMNRQIEDEARKRD-ELQR 433
Cdd:COG2268   229 EQEREIETARIAEA--EAELAKKKAEER-REAETA--RAEAEA-------AYEIAEANAEREVQRQLEIAEREREiELQE 296

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 193205629  434 IAEEKKRKQLLEDQcRAKQEKEKRDAEELEQMRLNIARLAGTKDVE 479
Cdd:COG2268   297 KEAEREEAELEADV-RKPAEAEKQAAEAEAEAEAEAIRAKGLAEAE 341

Smc

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

355-473

9.03e-06

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.94 E-value: 9.03e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  355 EAEEREHNLRIEKERHQKELEFRREALRKREQE---REEHKKRAQEELRRQMTAALEESTRRQAEMNRQIEDEARKRDEL 431
Cdd:COG1196   365 EALLEAEAELAEAEEELEELAEELLEALRAAAElaaQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL 444

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 193205629  432 QRIAEEKKRKQLLEDQCRAKQEkEKRDAEELEQMRLNIARLA 473
Cdd:COG1196   445 EEAAEEEAELEEEEEALLELLA-ELLEEAALLEAALAELLEE 485

TolA

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

346-461

9.47e-06

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

Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 49.27 E-value: 9.47e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  346 KERPSSPDSEAEEREHNLRIEKERHQKElEFRREALRKREQEREEH---KKRAQEELRRQMTAALEESTRRQAEMNRQIE 422
Cdd:COG3064     2 QEALEEKAAEAAAQERLEQAEAEKRAAA-EAEQKAKEEAEEERLAEleaKRQAEEEAREAKAEAEQRAAELAAEAAKKLA 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 193205629  423 DEARKRDELQRIAEEKKRKQLLEDQCRAKQEKEKRDAEE 461
Cdd:COG3064    81 EAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEK 119

tolA_full

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...

309-464

9.90e-06

Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 49.07 E-value: 9.90e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629   309 EKEKPRPTTENVVLKKVEMEKKRP----RSPELVPKK------IVMEKERPSSPDSEAEEREHNLRIEKERHQKELEFRR 378
Cdd:TIGR02794   62 AAKKEQERQKKLEQQAEEAEKQRAaeqaRQKELEQRAaaekaaKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAE 141

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629   379 -----EALRKREQEReehKKRAQEELRRQmtaalEESTRRQAEMNRQIEDEAR---KRDELQRIAEEKKRKQLLEDQCRA 450
Cdd:TIGR02794  142 rkakeEAAKQAEEEA---KAKAAAEAKKK-----AEEAKKKAEAEAKAKAEAEakaKAEEAKAKAEAAKAKAAAEAAAKA 213

                          170
                   ....*....|....
gi 193205629   451 KQEKEKRDAEELEQ 464
Cdd:TIGR02794  214 EAEAAAAAAAEAER 227

PRK05035

electron transport complex protein RnfC; Provisional

365-497

1.03e-05

electron transport complex protein RnfC; Provisional

Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 49.56 E-value: 1.03e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  365 IEKERHQKEL-----EFRREALRKREQEREEHKKRAQEELRRQMT----AALEESTRRQAEMNRQIEDEARKR-DELQRI 434
Cdd:PRK05035  441 IEQEKKKAEEakarfEARQARLEREKAAREARHKKAAEARAAKDKdavaAALARVKAKKAAATQPIVIKAGARpDNSAVI 520

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 193205629  435 AEEKKRKQLLEDQCRAKQEKEKRDAEElEQMRLNIARlAGTKDVENALKSPSLVEIVPPSDAR 497
Cdd:PRK05035  521 AAREARKAQARARQAEKQAAAAADPKK-AAVAAAIAR-AKAKKAAQQAANAEAEEEVDPKKAA 581

COG4913

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

355-473

1.03e-05

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

Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 1.03e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  355 EAEEREHNLRIEKERHQKELEFRREALRKREQEREEHKKRAqEELRRQMtaaLEESTRRQAEMNRQIEDEARKRDELQRI 434
Cdd:COG4913   285 FAQRRLELLEAELEELRAELARLEAELERLEARLDALREEL-DELEAQI---RGNGGDRLEQLEREIERLERELEERERR 360

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 193205629  435 AEEkkrkqlLEDQCRAKQEKEKRDAEELEQMRLNIARLA 473
Cdd:COG4913   361 RAR------LEALLAALGLPLPASAEEFAALRAEAAALL 393

Stathmin

pfam00836

Stathmin family; The Stathmin family of proteins play an important role in the regulation of ...

330-443

1.19e-05

Stathmin family; The Stathmin family of proteins play an important role in the regulation of the microtubule cytoskeleton. They regulate microtubule dynamics by promoting depolymerization of microtubules and/or preventing polymerization of tubulin heterodimers.

Pssm-ID: 459956 [Multi-domain] Cd Length: 136 Bit Score: 45.80 E-value: 1.19e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629   330 KRPRSPELVPKKIVMEKERPSSPDS------EAEEREHNLRIEKERHQ-KELEFRREALRKREQEREEHKKRAQEELRRQ 402
Cdd:pfam00836   22 KPPSVNAAPPKLSLSPKKKDSSLEEiqkkleAAEERRKSLEAQKLKQLaEKREKEEEALQKADEENNNFSKMAEEKLKQK 101

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 193205629   403 MTAALEestRRQAEMNRQIEdeaRKRDELQRIAEEKKRKQL 443
Cdd:pfam00836  102 MEAYKE---NREAQIAALKE---KLKEKEKHVEEVRKNKEQ 136

tolA_full

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...

386-483

1.55e-05

Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 48.30 E-value: 1.55e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629   386 QEREEHKKRAQEELRRQMTAALEESTRRQAEMNRQIEDEARKRDELQRIAEEKKRKQLLEDQC-----RAKQEKEKRDAE 460
Cdd:TIGR02794   57 QQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKqaeeaKAKQAAEAKAKA 136

                           90       100
                   ....*....|....*....|...
gi 193205629   461 ELEQMRLNIARLAGTKDVENALK 483
Cdd:TIGR02794  137 EAEAERKAKEEAAKQAEEEAKAK 159

DUF4659

pfam15558

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...

369-468

1.58e-05

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: 48.49 E-value: 1.58e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629   369 RHQKELEFRR---------EALRKREQER----EEHKKRAQEELRRQMTAALEEstrRQAEMNRQiEDEARKRDELQRIA 435
Cdd:pfam15558   16 RHKEEQRMRElqqqaalawEELRRRDQKRqetlERERRLLLQQSQEQWQAEKEQ---RKARLGRE-ERRRADRREKQVIE 91

                           90       100       110
                   ....*....|....*....|....*....|...
gi 193205629   436 EEKKRKQLLEDQCRAKQEKEKRDAEELEQMRLN 468
Cdd:pfam15558   92 KESRWREQAEDQENQRQEKLERARQEAEQRKQC 124

COG4372

Uncharacterized protein, contains DUF3084 domain [Function unknown];

354-472

3.04e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];

Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.59 E-value: 3.04e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  354 SEAEEREHNLRIEKERHQKELEFRREALRKREQEREEHKKRAQEeLRRQMTAALEESTRRQAEMNRQIEDEARKRDELQR 433
Cdd:COG4372    41 DKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEE-LNEQLQAAQAELAQAQEELESLQEEAEELQEELEE 119

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 193205629  434 IAEE----KKRKQLLEDQCRAKQEKEKRDAEELEQMRLNIARL 472
Cdd:COG4372   120 LQKErqdlEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162

PTZ00121

MAEBL; Provisional

291-458

3.13e-05

MAEBL; Provisional

Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.21 E-value: 3.13e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  291 KMRESESDDSVIIIPRKIEKEKPRPTTEnvvLKKVEmEKKRPRSPELVPKKivmEKERPSSPDSEAEEREHNLRIEKERH 370
Cdd:PTZ00121 1624 ELKKAEEEKKKVEQLKKKEAEEKKKAEE---LKKAE-EENKIKAAEEAKKA---EEDKKKAEEAKKAEEDEKKAAEALKK 1696

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  371 QKELEFRREALRKREQER----------EEHKKRAQEELRRQmtaalEESTRRQAEMNRQIEDEARKRDELQRIAEEKKR 440
Cdd:PTZ00121 1697 EAEEAKKAEELKKKEAEEkkkaeelkkaEEENKIKAEEAKKE-----AEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAE 1771

                         170
                  ....*....|....*...
gi 193205629  441 KQLLEDQCRAKQEKEKRD 458
Cdd:PTZ00121 1772 EIRKEKEAVIEEELDEED 1789

TPH

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...

355-472

4.54e-05

Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 46.84 E-value: 4.54e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629   355 EAEEREHNLRIEKERHQKEL-EFRREALRKREQEREEHKKRAQEELRRQMTAALEESTRRQAEMNRQIEDEARKRDELQR 433
Cdd:pfam13868  218 KERQKEREEAEKKARQRQELqQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEK 297

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 193205629   434 IAEEKKRKQLLEDQCRAKQEKEKRDAEELEQMRLNIARL 472
Cdd:pfam13868  298 QIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQ 336

PTZ00121

MAEBL; Provisional

278-446

5.61e-05

MAEBL; Provisional

Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.44 E-value: 5.61e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  278 IRPPETPKEPVKRKMRESESDDSVIIIPRKIEKEKP-----RPTTENVVLKKVEMEKKRPRSPELVPKKIVMEKERPSSP 352
Cdd:PTZ00121 1612 AKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKkaeelKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAA 1691

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  353 DSEAEEREHNLRIEKERHQKELEFRR-EALRKREQER----EEHKKRAQEELRRQMTAALEESTRRQ------------- 414
Cdd:PTZ00121 1692 EALKKEAEEAKKAEELKKKEAEEKKKaEELKKAEEENkikaEEAKKEAEEDKKKAEEAKKDEEEKKKiahlkkeeekkae 1771

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 193205629  415 ---AEMNRQIEDEARKRDELQRIAEEKKRKQLLED 446
Cdd:PTZ00121 1772 eirKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDN 1806

Smc

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

354-463

7.61e-05

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.85 E-value: 7.61e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  354 SEAEEREHNLRIEKERHQKELEFRREALRKREQEREEHKKRAQEELRRQMTAALEESTRRQAEMNRQIEDEARKRDELQR 433
Cdd:COG1196   671 LAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEE 750

                          90       100       110
                  ....*....|....*....|....*....|
gi 193205629  434 IAEEKKRKQLLEDQCRAKQEKEKRDAEELE 463
Cdd:COG1196   751 EALEELPEPPDLEELERELERLEREIEALG 780

TPH

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...

355-471

7.97e-05

Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 46.07 E-value: 7.97e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629   355 EAEEREhnLRIEKERHQKELEFRREALRKREQEREEHK-KRAQEELRRQMTAALEESTRRQAEMNRQI-----EDEARKR 428
Cdd:pfam13868  172 EAEREE--IEEEKEREIARLRAQQEKAQDEKAERDELRaKLYQEEQERKERQKEREEAEKKARQRQELqqareEQIELKE 249

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 193205629   429 DELQR-IAEEKKRKQLLEDQCRAKQEKEKRDAEELEQMRLNIAR 471
Cdd:pfam13868  250 RRLAEeAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRR 293

DUF5401

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

278-432

1.05e-04

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: 46.27 E-value: 1.05e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629   278 IRPPETPKEPVKRKMRESESDDSVIIIPR-KIEKEKPRPTTENVVLKKVEMEKKRPRSPELVPKKIVMEKERPSSPDSEA 356
Cdd:pfam17380  451 VRLEEQERQQQVERLRQQEEERKRKKLELeKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIY 530

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 193205629   357 EEREHNLRIEKERHQKELEFRRealRKREQEReehkkRAQEELRRQmtaaleESTRRQAEMNRQIEDEARKRDELQ 432
Cdd:pfam17380  531 EEERRREAEEERRKQQEMEERR---RIQEQMR-----KATEERSRL------EAMEREREMMRQIVESEKARAEYE 592

tolA

cell envelope integrity inner membrane protein TolA; Provisional

384-473

1.43e-04

cell envelope integrity inner membrane protein TolA; Provisional

Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 45.18 E-value: 1.43e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  384 REQEREEHKKRAQEELRRQMTAALEESTRRQAEmnrqiEDEARKRDELQRIAEEKKRKQlLEDQCRAKQEKEKRdAEELE 463
Cdd:PRK09510   66 RQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAA-----EQERLKQLEKERLAAQEQKKQ-AEEAAKQAALKQKQ-AEEAA 138

                          90
                  ....*....|
gi 193205629  464 QMRLNIARLA 473
Cdd:PRK09510  139 AKAAAAAKAK 148

PRK02224

DNA double-strand break repair Rad50 ATPase;

355-484

1.47e-04

DNA double-strand break repair Rad50 ATPase;

Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.80 E-value: 1.47e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  355 EAEEREHNLRIEKERHQKELEFRREALRKREQEREEH--------KKRAQEELRRQMTAALEESTRRQAEMNRQIEDEAR 426
Cdd:PRK02224  534 EKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAreevaelnSKLAELKERIESLERIRTLLAAIADAEDEIERLRE 613

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 193205629  427 KRDELQ--------RIAEEKKRKQLLE---DQCRAKQEKEKRD-AEE-LEQMRLNIARLAGTKD--------VENALKS 484
Cdd:PRK02224  614 KREALAelnderreRLAEKRERKRELEaefDEARIEEAREDKErAEEyLEQVEEKLDELREERDdlqaeigaVENELEE 692

MAD

pfam05557

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...

322-468

1.91e-04

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.

Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 45.50 E-value: 1.91e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629   322 LKKVEMEKKRPRspelvpkkIVMEKERPSSPDSEAEEREHNlriekerhqKELEFRREALRKREQEREEhKKRAQEELRR 401
Cdd:pfam05557   18 KKQMELEHKRAR--------IELEKKASALKRQLDRESDRN---------QELQKRIRLLEKREAEAEE-ALREQAELNR 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 193205629   402 QMTAALEESTRRQAEmNRQIEDEAR--------KRDELQRIAEEKK---RKQLLEDQCRAKQEKE-KRDAEELEQMRLN 468
Cdd:pfam05557   80 LKKKYLEALNKKLNE-KESQLADARevisclknELSELRRQIQRAElelQSTNSELEELQERLDLlKAKASEAEQLRQN 157

PTZ00121

MAEBL; Provisional

355-464

2.01e-04

MAEBL; Provisional

Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.52 E-value: 2.01e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  355 EAEEREHNLRIEKERHQKELEfRREALRKREQEREEHKKRAQEELRRQMTAALEESTR-----RQAEMNRQIEDEARKRD 429
Cdd:PTZ00121 1168 EARKAEDAKKAEAARKAEEVR-KAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKkaeavKKAEEAKKDAEEAKKAE 1246

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 193205629  430 ELQRIAE----EKKRKQLLEDQCRAKQEKEKRDAEELEQ 464
Cdd:PTZ00121 1247 EERNNEEirkfEEARMAHFARRQAAIKAEEARKADELKK 1285

Smc

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

363-473

2.07e-04

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.31 E-value: 2.07e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  363 LRIEKERHQKELEFRREALRKREQEREEHKKRAQEElrrqmTAALEESTRRQAEMNRQIEDEARKRDEL--------QRI 434
Cdd:COG1196   216 RELKEELKELEAELLLLKLRELEAELEELEAELEEL-----EAELEELEAELAELEAELEELRLELEELeleleeaqAEE 290

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 193205629  435 AEEKKRKQLLEDQCRAKQEKEKRDAEELEQMRLNIARLA 473
Cdd:COG1196   291 YELLAELARLEQDIARLEERRRELEERLEELEEELAELE 329

DR0291

COG1579

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...

353-503

2.07e-04

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

Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.15 E-value: 2.07e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  353 DSEAEEREHNLR-IEKERhqKELEFRREALRKREQEREEHKKRAQEELRR------QMTAALEESTRRQAE--------- 416
Cdd:COG1579    16 DSELDRLEHRLKeLPAEL--AELEDELAALEARLEAAKTELEDLEKEIKRleleieEVEARIKKYEEQLGNvrnnkeyea 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  417 MNRQIEDEARKR----DELQRIAEEKKRKQLLEDQCRAKQEKEKRDAEELEQmRLNiARLAGTKDVENAL--KSPSLVEI 490
Cdd:COG1579    94 LQKEIESLKRRIsdleDEILELMERIEELEEELAELEAELAELEAELEEKKA-ELD-EELAELEAELEELeaEREELAAK 171

                         170
                  ....*....|...
gi 193205629  491 VPPSDARAFEMIK 503
Cdd:COG1579   172 IPPELLALYERIR 184

Caldesmon

pfam02029

Caldesmon;

326-464

2.19e-04

Caldesmon;

Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 44.86 E-value: 2.19e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629   326 EMEKKRPRSPELVPKKIVMEKERPSSPDSEAEEREHNLRIE----KERHQKELEfRREALRKREQEREEHK-KRAQEELR 400
Cdd:pfam02029    6 EAARERRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEdselKPSGQGGLD-EEEAFLDRTAKREERRqKRLQEALE 84

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 193205629   401 RQ-----MTAALEESTRRQAEMNRQIE-----DEARKRDELQRIAEEKKRKQLLEDQCRAKQEKEKRDAEELEQ 464
Cdd:pfam02029   85 RQkefdpTIADEKESVAERKENNEEEEnssweKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEEEGEE 158

YhaN

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

355-474

2.38e-04

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 2.38e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  355 EAEEREHNLRIEK-ERHQKELEFRREALRKREQEREEHKKRAQEELRRQMTAALEESTRRQAEMNRQIEDEARKRDELQR 433
Cdd:COG4717   138 EAELAELPERLEElEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEE 217

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 193205629  434 IAEEKKRKQLLEDQCRAKQEKEKrDAEELEQMRLNIARLAG 474
Cdd:COG4717   218 AQEELEELEEELEQLENELEAAA-LEERLKEARLLLLIAAA 257

TPH

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...

344-473

2.53e-04

Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 44.52 E-value: 2.53e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629   344 MEKERPSSPDSEaEEREHNLRIEKERHQKELEFRREALRKREQEREEHKKRAQEELRRQMTAALEEstrRQAEMNRQIED 423
Cdd:pfam13868   49 MEEERERALEEE-EEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEE---DQAEAEEKLEK 124

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 193205629   424 EARKRDELQRIAEEK-------KRKQLLEDQ-----CRAKQEKEKRDAEELEQMR----LNIARLA 473
Cdd:pfam13868  125 QRQLREEIDEFNEEQaewkeleKEEEREEDErileyLKEKAEREEEREAEREEIEeekeREIARLR 190

Borrelia_P83

pfam05262

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

367-503

2.66e-04

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

Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 44.61 E-value: 2.66e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629   367 KERHQKELEFRREALRKREQEREEHKKRAQeELRRQMTAALEESTRRQAEMNRQIEDEARKRDELQRIAEEKKRkqlLED 446
Cdd:pfam05262  187 REDNEKGVNFRRDMTDLKERESQEDAKRAQ-QLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKN---LPK 262

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 193205629   447 QCRAKQEKEKRDAEELEQMRLNIARLAGTKDVENALKSpslveivppSDARAFEMIK 503
Cdd:pfam05262  263 PADTSSPKEDKQVAENQKREIEKAQIEIKKNDEEALKA---------KDHKAFDLKQ 310

YhaN

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

323-472

2.79e-04

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 2.79e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  323 KKVEMEKKRPRSPELVPKKI-VMEKERpsspdSEAEEREHNLRiEKERHQKELEFRREALRKREQEREEHKKRAQEEL-- 399
Cdd:COG4717    54 EADELFKPQGRKPELNLKELkELEEEL-----KEAEEKEEEYA-ELQEELEELEEELEELEAELEELREELEKLEKLLql 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  400 ------RRQMTAALEESTRRQAEMNRQIEDEARKRDELQRIAEEKKRKQ-----LLEDQCRAKQEKEKRDAEELEQMRLN 468
Cdd:COG4717   128 lplyqeLEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQeeleeLLEQLSLATEEELQDLAEELEELQQR 207


                  ....
gi 193205629  469 IARL 472
Cdd:COG4717   208 LAEL 211

TPH

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...

355-471

3.23e-04

Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 44.14 E-value: 3.23e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629   355 EAEEREHNLRIEKERhQKELEFRREALRKREQEREEHKK--RAQEELRRQMTAALEESTRRQAEMNRQIEDEARKRDELQ 432
Cdd:pfam13868   39 KEEERRLDEMMEEER-ERALEEEEEKEEERKEERKRYRQelEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAE 117

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 193205629   433 RIAEEKKRKQLLEDQCRAKQ------EKEKRDAEELEQMRLNIAR 471
Cdd:pfam13868  118 AEEKLEKQRQLREEIDEFNEeqaewkELEKEEEREEDERILEYLK 162

YhaN

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

354-484

3.31e-04

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 3.31e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  354 SEAEEREHNLRIEKERHQKELEFRREALRKREQEREEHKKRAQ--------EELRRQMtAALEESTRRQAEMNRQIEDEA 425
Cdd:COG4717    98 EELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAElaelperlEELEERL-EELRELEEELEELEAELAELQ 176

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 193205629  426 RKRDELQRIAEEKKRKQL---LEDQCRAKQEKEKRDAE------ELEQMRLNIARLAGTKDVENALKS 484
Cdd:COG4717   177 EELEELLEQLSLATEEELqdlAEELEELQQRLAELEEEleeaqeELEELEEELEQLENELEAAALEER 244

PTZ00121

MAEBL; Provisional

323-521

3.48e-04

MAEBL; Provisional

Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 3.48e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  323 KKVEMEKKRP---RSPELVPKKIVMEKERPSSPDSEAEEREHNLRIEKERHQKELEFRREA--------LRKREQER--E 389
Cdd:PTZ00121 1470 KKADEAKKKAeeaKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAeeakkadeAKKAEEKKkaD 1549

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  390 EHKK----RAQEELRRQMTAALEESTR----RQAEMNRQIEdEARKRDELQRIAEEKKRKQlleDQCRaKQEKEKRDAEE 461
Cdd:PTZ00121 1550 ELKKaeelKKAEEKKKAEEAKKAEEDKnmalRKAEEAKKAE-EARIEEVMKLYEEEKKMKA---EEAK-KAEEAKIKAEE 1624

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 193205629  462 L---EQMRLNIARLAGT-----KDVENALKSPSLVEIVPPSDARAFEMIKWNAVKCKIPENWEKRKDK 521
Cdd:PTZ00121 1625 LkkaEEEKKKVEQLKKKeaeekKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAE 1692

sbcc

TIGR00618

exonuclease SbcC; All proteins in this family for which functions are known are part of an ...

326-485

3.57e-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: 44.57 E-value: 3.57e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629   326 EMEKKRPRSPELVPKKIVMEKERPSSPdsEAEEREHNLRIEKERHQKELEFRrEALRKREQEREEHKKRAQEELRRQMTA 405
Cdd:TIGR00618  268 RIEELRAQEAVLEETQERINRARKAAP--LAAHIKAVTQIEQQAQRIHTELQ-SKMRSRAKLLMKRAAHVKQQSSIEEQR 344

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629   406 ALEESTRRQAEMNR-QIEDEARKRDELQRIAEEKKRKQLLEDQCRAKQEKEKRDAEELEQMRlniaRLAGTKDVENALKS 484
Cdd:TIGR00618  345 RLLQTLHSQEIHIRdAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQ----REQATIDTRTSAFR 420


                   .
gi 193205629   485 P 485
Cdd:TIGR00618  421 D 421

ATP-synt_Fo_b

cd06503

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...

355-443

3.69e-04

Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 41.65 E-value: 3.69e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  355 EAEEREHNLRIEKERHQKELEfrrEALRKREQEREEHKKRAQEELRRQMTAALEESTRRQAEMNRQIEDEARK-----RD 429
Cdd:cd06503    41 EAEKAKEEAEELLAEYEEKLA---EARAEAQEIIEEARKEAEKIKEEILAEAKEEAERILEQAKAEIEQEKEKalaelRK 117

                          90
                  ....*....|....
gi 193205629  430 ELQRIAEEKKRKQL 443
Cdd:cd06503   118 EVADLAVEAAEKIL 131

GBP_C

cd16269

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...

355-466

4.16e-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: 43.33 E-value: 4.16e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  355 EAEEREHnLRIEKERHQKElefRREALRKREQEREEHKKRAQEELRRQMTAALEESTRRQAEMNRQI----EDEARK-RD 429
Cdd:cd16269   180 EAEAEAI-LQADQALTEKE---KEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLkekmEEERENlLK 255

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 193205629  430 ELQRIAEEKKRKQ--LLEDQCRAKQEKEKrdaEELEQMR 466
Cdd:cd16269   256 EQERALESKLKEQeaLLEEGFKEQAELLQ---EEIRSLK 291

AtpF

COG0711

FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...

355-437

4.21e-04

FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase

Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 41.70 E-value: 4.21e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  355 EAEEREHNLRIEKERHQKELefrREALRKREQEREEHKKRAQEELRRQMTAALEESTRRQAEMNRQIEDEARK-RDELQR 433
Cdd:COG0711    42 EAERAKEEAEAALAEYEEKL---AEARAEAAEIIAEARKEAEAIAEEAKAEAEAEAERIIAQAEAEIEQERAKaLAELRA 118


                  ....
gi 193205629  434 IAEE 437
Cdd:COG0711   119 EVAD 122

tolA

cell envelope integrity inner membrane protein TolA; Provisional

353-464

4.85e-04

cell envelope integrity inner membrane protein TolA; Provisional

Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 43.64 E-value: 4.85e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  353 DSEAEEREHNLRIEKERHQKELEFRREALRKREQEREEHKKRAQEELRRQmtaaLEESTRRQAEMNRQIEDEARKRDELQ 432
Cdd:PRK09510   56 DPGAVVEQYNRQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQ----LEKERLAAQEQKKQAEEAAKQAALKQ 131

                          90       100       110
                  ....*....|....*....|....*....|..
gi 193205629  433 RIAEEKKRKQLLEDQCRAKQEkEKRDAEELEQ 464
Cdd:PRK09510  132 KQAEEAAAKAAAAAKAKAEAE-AKRAAAAAKK 162

SMC_prok_B

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...

326-474

5.69e-04

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.89 E-value: 5.69e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629   326 EMEKKRPRSPELvPKKIVMEKERPSSPDSEAEEREHNLRIEkERHQKELEFRREALRKREQEREEHKKRAQEELrrqmtA 405
Cdd:TIGR02168  713 ELEQLRKELEEL-SRQISALRKDLARLEAEVEQLEERIAQL-SKELTELEAEIEELEERLEEAEEELAEAEAEI-----E 785

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 193205629   406 ALEES-TRRQAEMNRQIEDEARKRDELQ----RIAEEKKRKQLLEDQCRAKQEKEKRDAEELEQMRLNIARLAG 474
Cdd:TIGR02168  786 ELEAQiEQLKEELKALREALDELRAELTllneEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA 859

PTZ00121

MAEBL; Provisional

345-461

5.97e-04

MAEBL; Provisional

Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 5.97e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  345 EKERPSSPDSEAEE--REHNLRIEKERHQKELEFRREALRKREQEREEHKKRAQEELRRQMTAALEESTRRQAEMNRQIE 422
Cdd:PTZ00121 1173 EDAKKAEAARKAEEvrKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNE 1252

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 193205629  423 ----------------------DEARKRDELQRIAEEKKRKQLLEDQCRAKQEKEKRDAEE 461
Cdd:PTZ00121 1253 eirkfeearmahfarrqaaikaEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEE 1313

YqiK

COG2268

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

364-469

6.04e-04

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

Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 43.32 E-value: 6.04e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  364 RIEKERHQKELEFRRE---ALRKREQEREEHKKRAQEELRRQMTAALE-ESTRRQAEMNRQIEDEARKRDELQRIAEEKK 439
Cdd:COG2268   196 EIIRDARIAEAEAEREteiAIAQANREAEEAELEQEREIETARIAEAEaELAKKKAEERREAETARAEAEAAYEIAEANA 275

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 193205629  440 RKQLLEDQCRAKQEK-----EKRDAEELEQMRLNI 469
Cdd:COG2268   276 EREVQRQLEIAEREReielqEKEAEREEAELEADV 310

TolA

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

328-508

6.24e-04

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

Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 43.49 E-value: 6.24e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  328 EKKRPRSPELVPK-KIVMEKERPSSPDSEAEEREHNLRIEKERHQKELEFRREALRKR---EQEREEHKKRAQEELRRQM 403
Cdd:COG3064    22 EAEKRAAAEAEQKaKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLaeaEKAAAEAEKKAAAEKAKAA 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  404 T----AALEESTRRQAEMNRQIEDEARKRDELQRIAEEKKRKQLLEDQCRAKQEKEKRDAEELEQMRLNIARLAGTKDVE 479
Cdd:COG3064   102 KeaeaAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAA 181

                         170       180
                  ....*....|....*....|....*....
gi 193205629  480 NALKSPSLVEIVPPSDARAFEMIKWNAVK 508
Cdd:COG3064   182 LVAAAAAAVEAADTAAAAAAALAAAAAAA 210

SMC_prok_B

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...

355-483

6.92e-04

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.89 E-value: 6.92e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629   355 EAEEREHNLRIE---KERHQKELEFRREALRKREQEREEHKKRAQEELRRqmtaaLEESTRRQAEMNRQIEDE-ARKRDE 430
Cdd:TIGR02168  688 ELEEKIAELEKAlaeLRKELEELEEELEQLRKELEELSRQISALRKDLAR-----LEAEVEQLEERIAQLSKElTELEAE 762

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 193205629   431 LQRIAEEKKRKQLLEDQCRAKQEKEKRDAEEL-EQMRLNIARLAGTKDVENALK 483
Cdd:TIGR02168  763 IEELEERLEEAEEELAEAEAEIEELEAQIEQLkEELKALREALDELRAELTLLN 816

TPH

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...

355-466

7.88e-04

Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 42.98 E-value: 7.88e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629   355 EAEEREHNLRIEKERHQKELEFRREALRKREQEREEHKKRAQEELRRQMTAAL---EESTRRQAEMNRQIEDEARKRDEL 431
Cdd:pfam13868  110 IQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKekaEREEEREAEREEIEEEKEREIARL 189

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 193205629   432 QRIAEEKKRKQLLEDQCRAKQEKEKRDAEELEQMR 466
Cdd:pfam13868  190 RAQQEKAQDEKAERDELRAKLYQEEQERKERQKER 224

SMC_N

pfam02463

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...

340-484

1.25e-03

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: 43.04 E-value: 1.25e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629   340 KKIVMEKERPSSPDSEAEEREHNLRIEKERHQKELEFRREALRKREQEREEHKKRAQEELRRQMTAALEESTRRQAE--- 416
Cdd:pfam02463  176 KKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEies 255

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 193205629   417 MNRQIEDEARKRDELQRIAEEKKRKQLLEDQCRAKQEKEKrdAEELEQMRLNIARLAGTKDVENALKS 484
Cdd:pfam02463  256 SKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEE--EELKSELLKLERRKVDDEEKLKESEK 321

GBP_C

pfam02841

Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...

365-463

1.29e-03

Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.

Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 41.89 E-value: 1.29e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629   365 IEKERHQKE-LEFRREALR---KREQEREEHKKRAQEELRRQMTAALEestrrqaemnrqiEDEARKRDELQRIAEEKKR 440
Cdd:pfam02841  206 IEAERAKAEaAEAEQELLRekqKEEEQMMEAQERSYQEHVKQLIEKME-------------AEREQLLAEQERMLEHKLQ 272

                           90       100
                   ....*....|....*....|....*
gi 193205629   441 KQ--LLEDQCRAKQEKEKRDAEELE 463
Cdd:pfam02841  273 EQeeLLKEGFKTEAESLQKEIQDLK 297

CAF-1_p150

pfam11600

Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...

324-438

1.37e-03

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: 40.44 E-value: 1.37e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629   324 KVEMEKKRPRSPELVPKKIVMEKERPSSPDSEAEEREHNLRIEKERHQKELEFRREALRKREQEREEHKKRAQEELRRQM 403
Cdd:pfam11600   13 KEKQRLEKDKERLRRQLKLEAEKEEKERLKEEAKAEKERAKEEARRKKEEEKELKEKERREKKEKDEKEKAEKLRLKEEK 92

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 193205629   404 TAALEESTRRQAEMNRQIEDEARKRDELQRIAEEK 438
Cdd:pfam11600   93 RKEKQEALEAKLEEKRKKEEEKRLKEEEKRIKAEK 127

DUF4659

pfam15558

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...

309-469

1.54e-03

Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 41.95 E-value: 1.54e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629   309 EKEKPRPTTENVVLKKVEMEKKRPR-SPElvpkkivmEKERPSSPDSEAEEREHNLRIEKERHQKElefRREALrKREQE 387
Cdd:pfam15558   49 ERERRLLLQQSQEQWQAEKEQRKARlGRE--------ERRRADRREKQVIEKESRWREQAEDQENQ---RQEKL-ERARQ 116

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629   388 REEHKKRAQEELRRqmtaALEESTRRQAEMNRQ-----IEDEARKRdeLQRIAEEKKRKQLLEDQCRAKQEKEKRD---- 458
Cdd:pfam15558  117 EAEQRKQCQEQRLK----EKEEELQALREQNSLqlqerLEEACHKR--QLKEREEQKKVQENNLSELLNHQARKVLvdcq 190

                          170
                   ....*....|..
gi 193205629   459 -AEELEQMRLNI 469
Cdd:pfam15558  191 aKAEELLRRLSL 202

GBP_C

cd16269

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...

354-452

1.57e-03

Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 41.79 E-value: 1.57e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  354 SEAEEREHNLRIEKERHQKELEFRREALRKREQEREEhKKRAQEELRRQMTAALEESTRR-QAEMNRQIEDEARKRDELQ 432
Cdd:cd16269   194 TEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLED-QERSYEEHLRQLKEKMEEERENlLKEQERALESKLKEQEALL 272

                          90       100
                  ....*....|....*....|
gi 193205629  433 RIAEEKKRkQLLEDQCRAKQ 452
Cdd:cd16269   273 EEGFKEQA-ELLQEEIRSLK 291

TolA

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

284-623

1.68e-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: 1.68e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  284 PKEPVKRKMRESESDdsviiipRKIEKEKPRPTTENVVLKKVEMEKKRPRSPELVPKKIVmEKERpsspdsEAEEREHNL 363
Cdd:COG3064    28 AAEAEQKAKEEAEEE-------RLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLA-EAEK------AAAEAEKKA 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  364 RIEKERHQKELEFRREALRKREQEREEHKKRAQEELRRQMTAALEESTRRQAEMNRQIEDEARKRDELQRIAEEKKRKQL 443
Cdd:COG3064    94 AAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAAR 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  444 LEDQCRAKQEKEKRDAEELEQMRLNIARLAGTKDVENALKSPSLVEIVPPSDARAFEMIKWNAVKCKIPENWEKRKDKFY 523
Cdd:COG3064   174 AAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAAD 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  524 RVFEWPSDAAQRDIERDEVVSIPRSKPIVIPQEDTYITRNRIPLKLPPKVKQAVPALVVRNSNNATRTVVAATVNENGIQ 603
Cdd:COG3064   254 LAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGG 333

                         330       340
                  ....*....|....*....|
gi 193205629  604 WPAETINIDEVVREIRGLMA 623
Cdd:COG3064   334 AASLEAALSLLAAGAAAAAA 353

SMC_prok_B

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...

354-466

1.85e-03

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 42.35 E-value: 1.85e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629   354 SEAEEREHNLRIEKERHQKELEFRREALRKREQEREEHKKRaqeelrrqmtaaLEESTRRQAEMNRQIEDEARKRDELQR 433
Cdd:TIGR02168  270 EELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRER------------LANLERQLEELEAQLEELESKLDELAE 337

                           90       100       110
                   ....*....|....*....|....*....|....
gi 193205629   434 IAEE-KKRKQLLEDQCRAKQEKEKRDAEELEQMR 466
Cdd:TIGR02168  338 ELAElEEKLEELKEELESLEAELEELEAELEELE 371

PRK02224

DNA double-strand break repair Rad50 ATPase;

354-477

1.98e-03

DNA double-strand break repair Rad50 ATPase;

Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 1.98e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  354 SEAEEREHNLRIEKERHQKELEFRREALRKREQEREEHKKRAQE------ELRRQMTAALEES----------TRRQAEM 417
Cdd:PRK02224  505 VEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAEleaeaeEKREAAAEAEEEAeeareevaelNSKLAEL 584

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  418 NRQIEDEARKRDELQRIAEEKKRKQLLEDQCRAKQEKEKRDAEELEQMRLNIARLAGTKD 477
Cdd:PRK02224  585 KERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFD 644

growth_prot_Scy

NF041483

polarized growth protein Scy;

354-470

2.03e-03

polarized growth protein Scy;

Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 42.12 E-value: 2.03e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  354 SEAEEREHNLRIEKErhqkelefrrEALRKREQEREEHKKRAQEELRRQMTAALEESTRRQAEMNRQIED-EARKRDELQ 432
Cdd:NF041483  509 TEAIERATTLRRQAE----------ETLERTRAEAERLRAEAEEQAEEVRAAAERAARELREETERAIAArQAEAAEELT 578

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 193205629  433 RI---AEEK--KRKQLLEDqCRAKQEKEKRDA-EELEQMRLNIA 470
Cdd:NF041483  579 RLhteAEERltAAEEALAD-ARAEAERIRREAaEETERLRTEAA 621

SMC_prok_A

TIGR02169

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...

355-470

2.44e-03

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

Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.98 E-value: 2.44e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629   355 EAEEREHNLRIEKERHQKElefRREALRKREQEREE----HKKRAQEELRRQMTAALEESTRRQAEMNRQIEDEARKRDE 430
Cdd:TIGR02169  193 IDEKRQQLERLRREREKAE---RYQALLKEKREYEGyellKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEE 269

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 193205629   431 LQRIAEE--KKRKQLLEDQCRAKQEKEKRDAEELEQMRLNIA 470
Cdd:TIGR02169  270 IEQLLEElnKKIKDLGEEEQLRVKEKIGELEAEIASLERSIA 311

Smc

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

377-472

2.53e-03

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.85 E-value: 2.53e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  377 RREALRKRE--QEREEhkkRAQ---EELRRQMtAALEEStRRQAEMNRQIEDEARKRD-EL---------QRIAEEKKRK 441
Cdd:COG1196   174 KEEAERKLEatEENLE---RLEdilGELERQL-EPLERQ-AEKAERYRELKEELKELEaELlllklreleAELEELEAEL 248

                          90       100       110
                  ....*....|....*....|....*....|.
gi 193205629  442 QLLEDQCRAKQEKEKRDAEELEQMRLNIARL 472
Cdd:COG1196   249 EELEAELEELEAELAELEAELEELRLELEEL 279

COG2433

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];

344-466

3.08e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];

Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.38 E-value: 3.08e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  344 MEKERPSSPDSEAEEREHNLRIEKERHQ-KELEFRREALRKREQEREEHKKRAQEELRRqmtaaleestrrqaeMNRQIE 422
Cdd:COG2433   394 EPEAEREKEHEERELTEEEEEIRRLEEQvERLEAEVEELEAELEEKDERIERLERELSE---------------ARSEER 458

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 193205629  423 DEARKRDELQRIAEEKKRkqlLEDQCRAKQEKEKRDAEELEQMR 466
Cdd:COG2433   459 REIRKDREISRLDREIER---LERELEEERERIEELKRKLERLK 499

HlpA

COG2825

Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...

353-439

3.18e-03

Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];

Pssm-ID: 442073 [Multi-domain] Cd Length: 171 Bit Score: 39.43 E-value: 3.18e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  353 DSEAEEREHNLRIEKERHQKELEFRREALRkreQEREEHKKRAQEELRRQMTAALEESTRRQAEMNRQIEDEARKrdELQ 432
Cdd:COG2825    56 QAELQKLEKELQALQEKLQKEAATLSEEER---QKKERELQKKQQELQRKQQEAQQDLQKRQQELLQPILEKIQK--AIK 130


                  ....*..
gi 193205629  433 RIAEEKK 439
Cdd:COG2825   131 EVAKEEG 137

TPH

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...

355-473

3.19e-03

Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 41.06 E-value: 3.19e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629   355 EAEEREhNLRIEkeRHQKELEFRRealRKREQEREEHKKRAQEELRRQMTAALEESTRRQA-------EMNRQIEDEARK 427
Cdd:pfam13868  199 EKAERD-ELRAK--LYQEEQERKE---RQKEREEAEKKARQRQELQQAREEQIELKERRLAeeaereeEEFERMLRKQAE 272

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 193205629   428 RDELQRIAEEKKR------KQLLEDQCRAKQEKEKRDAEELEQMRLNIARLA 473
Cdd:pfam13868  273 DEEIEQEEAEKRRmkrlehRRELEKQIEEREEQRAAEREEELEEGERLREEE 324

PRK03918

DNA double-strand break repair ATPase Rad50;

285-476

3.43e-03

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 3.43e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  285 KEPVKRKMRESEsdDSVIIIPRKI-EKEKPRPTTEnvvlKKVEMEKKRPRSPELVPKKIVMEKERPSSPDSEAEEREHNL 363
Cdd:PRK03918  188 TENIEELIKEKE--KELEEVLREInEISSELPELR----EELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKI 261

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  364 RiEKERHQKELEFRREALRKREQEREEHKKRAQE-----ELRRQMTAALEESTRRQAEMNRQIEDEARKRDELQRIAEEK 438
Cdd:PRK03918  262 R-ELEERIEELKKEIEELEEKVKELKELKEKAEEyiklsEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERL 340

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 193205629  439 KRKQLLEDQCRAKQEKEKRDAEELEQMRLNIARLAGTK 476
Cdd:PRK03918  341 EELKKKLKELEKRLEELEERHELYEEAKAKKEELERLK 378

PRK02224

DNA double-strand break repair Rad50 ATPase;

355-472

3.77e-03

DNA double-strand break repair Rad50 ATPase;

Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.18 E-value: 3.77e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  355 EAEEREHNLRIEKERHQKE-LEFRREALRKREQEREEHKKRAqEELRRQMTAALEESTRRQAEMNRQIEDEARKRDELQR 433
Cdd:PRK02224  460 PVEGSPHVETIEEDRERVEeLEAELEDLEEEVEEVEERLERA-EDLVEAEDRIERLEERREDLEELIAERRETIEEKRER 538

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 193205629  434 IAEEKKRKQLLEDQCRAKQEKEKRDAEELEQMRLNIARL 472
Cdd:PRK02224  539 AEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAEL 577

PRK07352

F0F1 ATP synthase subunit B; Validated

374-484

3.95e-03

F0F1 ATP synthase subunit B; Validated

Pssm-ID: 180941 [Multi-domain] Cd Length: 174 Bit Score: 39.17 E-value: 3.95e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  374 LEFRREALRKREQEREEHKKRAQEEL---RRQMTAALEEstrrqAEmnrQIEDEARKRDELQRIAEEKKRKQLLEdqcRA 450
Cdd:PRK07352   48 LEERREAILQALKEAEERLRQAAQALaeaQQKLAQAQQE-----AE---RIRADAKARAEAIRAEIEKQAIEDMA---RL 116

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 193205629  451 KQEKEKR-DAEE---LEQMRLNIARLAGTKdVENALKS 484
Cdd:PRK07352  117 KQTAAADlSAEQervIAQLRREAAELAIAK-AESQLPG 153

OmpH

smart00935

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...

353-439

4.13e-03

Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 38.72 E-value: 4.13e-03

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629    353 DSEAEEREHNLRIEKERHQKELEFRREALRkreQEREEHKKRAQEELRRQMTAALEESTRRQAEMNRQIEDEARKrdELQ 432
Cdd:smart00935   31 QAELEKLEKELQKLKEKLQKDAATLSEAAR---EKKEKELQKKVQEFQRKQQKLQQDLQKRQQEELQKILDKINK--AIK 105


                    ....*..
gi 193205629    433 RIAEEKK 439
Cdd:smart00935  106 EVAKKKG 112

SMC_prok_A

TIGR02169

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...

363-484

4.61e-03

Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.21 E-value: 4.61e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629   363 LRIEKERHQKELEFRREALRKREQEREEHKKR--AQEELRRQMTAALEESTR-RQAEMNRQIEDEARKRDELQRIAEEKK 439
Cdd:TIGR02169  235 LERQKEAIERQLASLEEELEKLTEEISELEKRleEIEQLLEELNKKIKDLGEeEQLRVKEKIGELEAEIASLERSIAEKE 314

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 193205629   440 RKQLLEDQCRAKQEKE-KRDAEELEQMRLNIARLAGTKD-VENALKS 484
Cdd:TIGR02169  315 RELEDAEERLAKLEAEiDKLLAEIEELEREIEEERKRRDkLTEEYAE 361

SMC_prok_A

TIGR02169

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...

289-494

4.61e-03

Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.21 E-value: 4.61e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629   289 KRKMRESESDDSviIIPRKIEKEKPRPTTENVVLKKVEMEKKRPRS------PELVPKKIVMEKERPSSPDSEAEEREHN 362
Cdd:TIGR02169  715 SRKIGEIEKEIE--QLEQEEEKLKERLEELEEDLSSLEQEIENVKSelkeleARIEELEEDLHKLEEALNDLEARLSHSR 792

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629   363 LR-IEKERHQKELEFRREALRKREQEREEHKKRAQEELRRQMTAALEESTR----RQAEMNRQIEDEARKRDELQRIAEE 437
Cdd:TIGR02169  793 IPeIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIdlkeQIKSIEKEIENLNGKKEELEEELEE 872

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 193205629   438 KK------RKQL---------LEDQCRAKQEKEKRDAEELEQMRLNIARLAGTKDV---ENALKSPSLVEIVPPS 494
Cdd:TIGR02169  873 LEaalrdlESRLgdlkkerdeLEAQLRELERKIEELEAQIEKKRKRLSELKAKLEAleeELSEIEDPKGEDEEIP 947

SMC_N

pfam02463

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...

289-465

4.86e-03

Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.11 E-value: 4.86e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629   289 KRKMRESESDDSVIIIPRKIEKEKprpttenvvLKKVEMEKKRPRSPELVPKKIVM-EKERPSSPDSEAEEREHNLR--- 364
Cdd:pfam02463  176 KKLIEETENLAELIIDLEELKLQE---------LKLKEQAKKALEYYQLKEKLELEeEYLLYLDYLKLNEERIDLLQell 246

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629   365 ------IEKERHQKELEFRREALRKREQEREEHKKRAQEELRRQMTAALEE--STRRQAEMNRQIEDEARKRDELQ---R 433
Cdd:pfam02463  247 rdeqeeIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEElkSELLKLERRKVDDEEKLKESEKEkkkA 326

                          170       180       190
                   ....*....|....*....|....*....|..
gi 193205629   434 IAEEKKRKQLLEDQCRAKQEKEKRDAEELEQM 465
Cdd:pfam02463  327 EKELKKEKEEIEELEKELKELEIKREAEEEEE 358

mS26_PET12

cd23703

Saccharomyces cerevisiae mitochondrial small ribosomal subunit protein mS26 and similar ...

312-459

4.86e-03

Saccharomyces cerevisiae mitochondrial small ribosomal subunit protein mS26 and similar proteins; mS26, also known as mitochondrial 37S ribosomal protein PET12, is a component of the mitochondrial small ribosomal subunit (mt-SSU) of Saccharomyces cerevisiae mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane. The family also includes a group of uncharacterized proteins from pezizomycotina, which show high sequence similarity with mS26.

Pssm-ID: 467916 [Multi-domain] Cd Length: 179 Bit Score: 39.07 E-value: 4.86e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  312 KPRPttenvVLKKveMEKKRPRSPELVpKKIV---MEKERPSSPDSEAEE---------REH---NLRIEKERHQKELEF 376
Cdd:cd23703     9 VPRE-----IFKR--PTRKDKTVEEYI-AKTTpepKKEPKPKSPLSEYQEwkrkmaelrRQNlreGLRELEERKLKTEEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  377 RREALRKREQEREEHKKRAQEELRRQMTAALEESTRrqAEMNRQIEDEARKrdelQRIAEEKKRKQLLEdqcrAKQEKEK 456
Cdd:cd23703    81 RAKRSERKQAERERALNAPEREDERLTLPTIESALL--GPLMRVRTDPERE----ERAAKRRANREAKE----LAKKEAR 150


                  ...
gi 193205629  457 RDA 459
Cdd:cd23703   151 ADA 153

SMC_N

pfam02463

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...

340-464

4.98e-03

Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.11 E-value: 4.98e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629   340 KKIVMEKERPSSPDSEAEEREHNLRIEKERHQKELefRREALRKREQEREEHKKRAQEELRRQMTAALEESTRRQAEMNR 419
Cdd:pfam02463  745 IDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEE--REKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQL 822

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 193205629   420 QIEDEARKRDELqrIAEEKKRKQLLEDQCRAKQEKEKRDAEELEQ 464
Cdd:pfam02463  823 LIEQEEKIKEEE--LEELALELKEEQKLEKLAEEELERLEEEITK 865

SMC_prok_B

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...

340-484

5.60e-03

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.81 E-value: 5.60e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629   340 KKIVMEKERPSSPDSEAEEREHNLRiEKERHQKELEFRREALRKREQEREEHKKRAQEELRRqMTAALEESTRRQAEMNR 419
Cdd:TIGR02168  302 QQKQILRERLANLERQLEELEAQLE-ELESKLDELAEELAELEEKLEELKEELESLEAELEE-LEAELEELESRLEELEE 379

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 193205629   420 QIEDEARKRD-----------ELQRIAEEKkrKQLLEDQCRAKQEKEKRDAEELE-QMRLNIARLAGTKDVENALKS 484
Cdd:TIGR02168  380 QLETLRSKVAqlelqiaslnnEIERLEARL--ERLEDRRERLQQEIEELLKKLEEaELKELQAELEELEEELEELQE 454

EnvC

COG4942

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...

368-459

5.81e-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: 40.13 E-value: 5.81e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  368 ERHQKELEFRREALRKREQEREEHKKRAQEElRRQMTAALEESTRRQAEMNRQIEDEARKRDELQRiaEEKKRKQLLEDQ 447
Cdd:COG4942   156 RADLAELAALRAELEAERAELEALLAELEEE-RAALEALKAERQKLLARLEKELAELAAELAELQQ--EAEELEALIARL 232

                          90
                  ....*....|..
gi 193205629  448 CRAKQEKEKRDA 459
Cdd:COG4942   233 EAEAAAAAERTP 244

EnvC

COG4942

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...

366-503

5.96e-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: 40.13 E-value: 5.96e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  366 EKERHQKELEFRREALRKREQEREEHKKRAQEELRR------QMTAALEESTRRQAEMNRQIEDEARKRDELQriAEEKK 439
Cdd:COG4942    24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAlerriaALARRIRALEQELAALEAELAELEKEIAELR--AELEA 101

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 193205629  440 RKQLLEDQCRAKQEKEKRDAEELeqmrlniarLAGTKDVENALKSPSLVEIVPPSDARAFEMIK 503
Cdd:COG4942   102 QKEELAELLRALYRLGRQPPLAL---------LLSPEDFLDAVRRLQYLKYLAPARREQAEELR 156

TAF4

pfam05236

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

316-441

6.02e-03

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: 39.56 E-value: 6.02e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629   316 TTENVVLKKVEMEKKRP-RSPELVPKKI--VMEKERPSSPDSE--------AEER------------EHNLRIEKERHQK 372
Cdd:pfam05236   27 TNSEAVGTVVRSCKDEPfLNPYPLQRKIleIAKKNGLKEIDPDvlellshaCEERlrnlleklivisRHRRDGEKTDHRY 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629   373 EL--EFRREaLRKREQ-EREEHKKRAQEELRRQMTAALEEST----------RRQAEMNRQIEDEARKRDE----LQRIA 435
Cdd:pfam05236  107 EQtsDVRKQ-LKFLAQkDKEEEERRVAEEREGLLKAAKSRSNqedpeqlklkQEAKEMQKEEDEKMRHRAAnltaLAAIG 185


                   ....*.
gi 193205629   436 EEKKRK 441
Cdd:pfam05236  186 PRKKKY 191

SMC_prok_B

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...

354-475

6.20e-03

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.81 E-value: 6.20e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629   354 SEAEEREHNLRIE---KERHQKELEFRREALRKREQEREEHKKRAQEELrrqmtaaleestrrqAEMNRQIEDEARKRDE 430
Cdd:TIGR02168  806 DELRAELTLLNEEaanLRERLESLERRIAATERRLEDLEEQIEELSEDI---------------ESLAAEIEELEELIEE 870

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 193205629   431 LQR-----------------------------IAEEKKRKQLLEDQCRAKQEKEKRDAEELEQMRLNIARLAGT 475
Cdd:TIGR02168  871 LESeleallnerasleealallrseleelseeLRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQER 944

PRK00106

ribonuclease Y;

354-473

6.33e-03

ribonuclease Y;

Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 40.24 E-value: 6.33e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  354 SEAEEREHNLRIEKER----HQKE--LEFRREALRKREQEREEHKKRAQEelRRQMTAALeesTRRQAEMNRQIEDEARK 427
Cdd:PRK00106   49 GKAERDAEHIKKTAKReskaLKKEllLEAKEEARKYREEIEQEFKSERQE--LKQIESRL---TERATSLDRKDENLSSK 123

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 193205629  428 RDELQriaeekKRKQLLEDQCRAKQEKEKRDAEELEQMRLNIARLA 473
Cdd:PRK00106  124 EKTLE------SKEQSLTDKSKHIDEREEQVEKLEEQKKAELERVA 163

PRK12705

hypothetical protein; Provisional

341-473

6.86e-03

hypothetical protein; Provisional

Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 40.08 E-value: 6.86e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  341 KIVMEKERPSSPDSEAEEREHNLRIEKERHQKELEFRREALR-KREQEREEHKKRAQEELRRQMTAALEESTRRQAEMNR 419
Cdd:PRK12705   37 RILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREElQREEERLVQKEEQLDARAEKLDNLENQLEEREKALSA 116

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 193205629  420 Q----IEDEARKRDELQRIA---EEKKRKQLLED-QCRAKQEKEKRDAEELEQMRLNIARLA 473
Cdd:PRK12705  117 RelelEELEKQLDNELYRVAgltPEQARKLLLKLlDAELEEEKAQRVKKIEEEADLEAERKA 178

UPF0242

pfam06785

Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ...

321-449

7.31e-03

Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal transmembrane region and a C-terminal coiled-coil.

Pssm-ID: 429117 [Multi-domain] Cd Length: 194 Bit Score: 38.65 E-value: 7.31e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629   321 VLKKVEMEKKRPRSPELVPKKIVMEKERPSSPDSEAEEREHNLRIEKERHQKELEFRREALRKREQEREEHKKRAQEeLR 400
Cdd:pfam06785   53 LLYYWEDALKEKFEKSFLEEKEAKLTELDAEGFKILEETLEELQSEEERLEEELSQKEEELRRLTEENQQLQIQLQQ-IS 131

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 193205629   401 RQMTAALEESTRRQAEMNRQIeDEARKRDELQRIAEEKKRKQL--LEDQCR 449
Cdd:pfam06785  132 QDFAEFRLESEEQLAEKQLLI-NEYQQTIEEQRSVLEKRQDQIenLESKVR 181

mukB

PRK04863

chromosome partition protein MukB;

345-474

7.51e-03

chromosome partition protein MukB;

Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.33 E-value: 7.51e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  345 EKERPSSPDSEAEEREHnlRIEKERHQKELEFRREALRKREQEREEHKKRAqEELRRQMTAALEESTRRQAEMNRQIEDE 424
Cdd:PRK04863  564 EARLESLSESVSEARER--RMALRQQLEQLQARIQRLAARAPAWLAAQDAL-ARLREQSGEEFEDSQDVTEYMQQLLERE 640

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 193205629  425 ARKRDELQRIAEekkRKQLLEDQCRakqEKEKRDAEELEQMRLNIARLAG 474
Cdd:PRK04863  641 RELTVERDELAA---RKQALDEEIE---RLSQPGGSEDPRLNALAERFGG 684

PRK00247

putative inner membrane protein translocase component YidC; Validated

375-492

8.04e-03

putative inner membrane protein translocase component YidC; Validated

Pssm-ID: 178945 [Multi-domain] Cd Length: 429 Bit Score: 39.83 E-value: 8.04e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  375 EFRREALRKREQEREE-HKKRAQEELRRQMTAALEESTRRQAEMNRQIEDEARKRDElqRIAEEKKRKQLLEDQCRAKQE 453
Cdd:PRK00247  282 EFKEHHAEQRAQYREKqKEKKAFLWTLRRNRLRMIITPWRAPELHAENAEIKKTRTA--EKNEAKARKKEIAQKRRAAER 359

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 193205629  454 K--EKRDAEELEQMRLNIARLAGTKDVENALKSPSLVEIVP 492
Cdd:PRK00247  360 EinREARQERAAAMARARARRAAVKAKKKGLIDASPNEDTP 400

YhaN

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

354-472

8.41e-03

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 8.41e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629  354 SEAEEREHNLRIEKERHQKELEFRR------EALRKR-EQEREEHKKRAQ-EELRRQMTAALEESTRRQAEMNR-QIEDE 424
Cdd:COG4717   354 REAEELEEELQLEELEQEIAALLAEagvedeEELRAAlEQAEEYQELKEElEELEEQLEELLGELEELLEALDEeELEEE 433

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 193205629  425 -ARKRDELQRIAEEkkRKQLLEDQCRAKQEKEK-RDAEELEQMRLNIARL 472
Cdd:COG4717   434 lEELEEELEELEEE--LEELREELAELEAELEQlEEDGELAELLQELEEL 481

CR6_interact

pfam10147

Growth arrest and DNA-damage-inducible proteins-interacting protein 1; Members of this family ...

355-465

8.64e-03

Growth arrest and DNA-damage-inducible proteins-interacting protein 1; Members of this family of proteins act as negative regulators of G1 to S cell cycle phase progression by inhibiting cyclin-dependent kinases. Inhibitory effects are additive with GADD45 proteins but occur also in the absence of GADD45 proteins. Furthermore, they act as a repressor of the orphan nuclear receptor NR4A1 by inhibiting AB domain-mediated transcriptional activity.

Pssm-ID: 431088 [Multi-domain] Cd Length: 204 Bit Score: 38.68 E-value: 8.64e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193205629   355 EAEEREHNLRIEKerHQKELEFRREALRKREQEREEHKKRAQEELrRQMTAALEESTR-RQAEMNRQIEDEARKRDELQ- 432
Cdd:pfam10147   79 EAEEREWYPSLAQ--MLESNRAQKAEKEARRQAREQEIAKKMAKM-PQWIADWNAQKAkREAEAQAAKERKERLVAEARe 155

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 193205629   433 --------RIAEEKKRKQLLEDQCRAKQEKEKRDAEELEQM 465
Cdd:pfam10147  156 hfgfkvdpRDERFKEMLQQKEKEDKKKVKEAKRKEKEEKRM 196

SMC_prok_B