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Conserved domains on  [gi|597837628|gb|EYB87253|]
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hypothetical protein Y032_0266g716 [Ancylostoma ceylanicum]

Protein Classification

DUF5401 domain-containing protein( domain architecture ID 1000055)

DUF5401 domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DUF5401 super family cl38662
Family of unknown function (DUF5401); This is a family of unknown function found in ...
39-696 1.06e-43

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


The actual alignment was detected with superfamily member pfam17380:

Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 169.92  E-value: 1.06e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   39 EEFIFSTKRPKRPRPKTKAASStltaaptsaasssthpstttptpTVAFPTPALLPTPEPTTVRPYRPVFTTPNRKIVSS 118
Cdd:pfam17380 101 EEFVFSTIRPKSRKPKARTRGK-----------------------KRKTTTTMIQTTTPMMVTTSSSALEMTTTPKIVIF 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  119 AATKSPKPPPTRTTATTLTTPPLKNRKV------------TEPIPVSEA---------------QMTGMQPSTRGYT--- 168
Cdd:pfam17380 158 ASKKNASGGNRSGEQRKQIQLIRRRRGNhsaftrpgrprtTTPMPVTHAtrfvpgiqmstvapkEVQGMPHTLAPYEkme 237
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  169 RGPQMHTTGVTAGTTSGEHMVNYKGITMSEDEFLKQLVRIVEaHQVAINKIEEQvgeerrrggvEDHEHPAGSFRKQGPS 248
Cdd:pfam17380 238 RRKESFNLAEDVTTMTPEYTVRYNGQTMTENEFLNQLLHIVQ-HQKAVSERQQQ----------EKFEKMEQERLRQEKE 306
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  249 GNFEEGSSNAEMEQLERQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQMAEMqraqkemew 328
Cdd:pfam17380 307 EKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERIRQEEIAMEISRM--------- 377
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  329 qREIARQKAEMDEKEkqrqveiarqmaERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVERKKQEEVRRIEKAR 408
Cdd:pfam17380 378 -RELERLQMERQQKN------------ERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEER 444
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  409 KKsemeKKERERQQEIARQHaERQRKEEEARRQEEARLFAERQKKERERQEEIARQMEEEEKRQREEAEKEEMRKRKIEE 488
Cdd:pfam17380 445 AR----EMERVRLEEQERQQ-QVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLE 519
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  489 ERLRKEEEQRIEAQ--RKAEEERRIEEQLAARE---------VENQSTVVNPAFGMHIPGETQAGEHSTDYYGYSTNSDA 557
Cdd:pfam17380 520 KEMEERQKAIYEEErrREAEEERRKQQEMEERRriqeqmrkaTEERSRLEAMEREREMMRQIVESEKARAEYEATTPITT 599
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  558 TKTVlaglmsMSSRLTSTEPPQLE--IIHFTAPPPtpsspanEWVT-SPHSWRPPPDMQTNVLEWSRTPIpstgtselps 634
Cdd:pfam17380 600 IKPI------YRPRISEYQPPDVEshMIRFTTQSP-------EWATpSPATWNPEWNTVTAEEETPGIPI---------- 656
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 597837628  635 tVTSECDSNVECAFSYEDDLLCPHPNDATRYLQCTPMIGRRGRWTERMCPPNLVFIPSYGRC 696
Cdd:pfam17380 657 -IHSQCQVNGECELKYDSDSFCAHPSNPSMYLQCAPLYGRLGRWTERHCPDTLIFIVSIGRC 717
 
Name Accession Description Interval E-value
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
39-696 1.06e-43

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: 169.92  E-value: 1.06e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   39 EEFIFSTKRPKRPRPKTKAASStltaaptsaasssthpstttptpTVAFPTPALLPTPEPTTVRPYRPVFTTPNRKIVSS 118
Cdd:pfam17380 101 EEFVFSTIRPKSRKPKARTRGK-----------------------KRKTTTTMIQTTTPMMVTTSSSALEMTTTPKIVIF 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  119 AATKSPKPPPTRTTATTLTTPPLKNRKV------------TEPIPVSEA---------------QMTGMQPSTRGYT--- 168
Cdd:pfam17380 158 ASKKNASGGNRSGEQRKQIQLIRRRRGNhsaftrpgrprtTTPMPVTHAtrfvpgiqmstvapkEVQGMPHTLAPYEkme 237
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  169 RGPQMHTTGVTAGTTSGEHMVNYKGITMSEDEFLKQLVRIVEaHQVAINKIEEQvgeerrrggvEDHEHPAGSFRKQGPS 248
Cdd:pfam17380 238 RRKESFNLAEDVTTMTPEYTVRYNGQTMTENEFLNQLLHIVQ-HQKAVSERQQQ----------EKFEKMEQERLRQEKE 306
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  249 GNFEEGSSNAEMEQLERQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQMAEMqraqkemew 328
Cdd:pfam17380 307 EKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERIRQEEIAMEISRM--------- 377
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  329 qREIARQKAEMDEKEkqrqveiarqmaERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVERKKQEEVRRIEKAR 408
Cdd:pfam17380 378 -RELERLQMERQQKN------------ERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEER 444
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  409 KKsemeKKERERQQEIARQHaERQRKEEEARRQEEARLFAERQKKERERQEEIARQMEEEEKRQREEAEKEEMRKRKIEE 488
Cdd:pfam17380 445 AR----EMERVRLEEQERQQ-QVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLE 519
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  489 ERLRKEEEQRIEAQ--RKAEEERRIEEQLAARE---------VENQSTVVNPAFGMHIPGETQAGEHSTDYYGYSTNSDA 557
Cdd:pfam17380 520 KEMEERQKAIYEEErrREAEEERRKQQEMEERRriqeqmrkaTEERSRLEAMEREREMMRQIVESEKARAEYEATTPITT 599
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  558 TKTVlaglmsMSSRLTSTEPPQLE--IIHFTAPPPtpsspanEWVT-SPHSWRPPPDMQTNVLEWSRTPIpstgtselps 634
Cdd:pfam17380 600 IKPI------YRPRISEYQPPDVEshMIRFTTQSP-------EWATpSPATWNPEWNTVTAEEETPGIPI---------- 656
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 597837628  635 tVTSECDSNVECAFSYEDDLLCPHPNDATRYLQCTPMIGRRGRWTERMCPPNLVFIPSYGRC 696
Cdd:pfam17380 657 -IHSQCQVNGECELKYDSDSFCAHPSNPSMYLQCAPLYGRLGRWTERHCPDTLIFIVSIGRC 717
PTZ00121 PTZ00121
MAEBL; Provisional
252-521 4.45e-23

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 106.38  E-value: 4.45e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  252 EEGSSNAEMEQLERQRQQEIARQVAERQQKErEELEWQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEWQRE 331
Cdd:PTZ00121 1363 EEKAEAAEKKKEEAKKKADAAKKKAEEKKKA-DEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAE 1441
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  332 IARQKAEMDEK-EKQRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQK---EIARQVVERKKQEEVRRIEKA 407
Cdd:PTZ00121 1442 EAKKADEAKKKaEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKkadEAKKAAEAKKKADEAKKAEEA 1521
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  408 RKKSEMEKKERERQQEIARQHAERQR----KEEEARRQEEARLFAERQKKERE------RQEEIARQMEEEEKRQREEAE 477
Cdd:PTZ00121 1522 KKADEAKKAEEAKKADEAKKAEEKKKadelKKAEELKKAEEKKKAEEAKKAEEdknmalRKAEEAKKAEEARIEEVMKLY 1601
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 597837628  478 KEEmRKRKIEEERLRKEEEQRIEAQRKAEEERRIEEQLAAREVE 521
Cdd:PTZ00121 1602 EEE-KKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAE 1644
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
252-522 1.52e-19

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 94.23  E-value: 1.52e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 252 EEGSSNAEMEQLERQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEwqRE 331
Cdd:COG1196  289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE--EA 366
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 332 IARQKAEMDEKEKQRQvEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVERKKQEEVRRIEKARKKS 411
Cdd:COG1196  367 LLEAEAELAEAEEELE-ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 412 EMEKKERERQQEIARQHAERQRKEEEARRQEearlfAERQKKERERQEEIARQMEEEEKRQREEAEKEEMRKRKIEEERL 491
Cdd:COG1196  446 EAAEEEAELEEEEEALLELLAELLEEAALLE-----AALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLR 520
                        250       260       270
                 ....*....|....*....|....*....|.
gi 597837628 492 RKEEEQRIEAQRKAEEERRIEEQLAAREVEN 522
Cdd:COG1196  521 GLAGAVAVLIGVEAAYEAALEAALAAALQNI 551
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
202-464 8.20e-12

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: 69.32  E-value: 8.20e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   202 LKQLVRIVEAHQVAINKIEEQVgEERRRGGVEDHEhpagsfRKQGPSGNFEEgsSNAEMEQLErqrqQEIARQVAERQQK 281
Cdd:TIGR02168  248 LKEAEEELEELTAELQELEEKL-EELRLEVSELEE------EIEELQKELYA--LANEISRLE----QQKQILRERLANL 314
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   282 EREELEWQQEIARQEAERQRKEEEM-RRQQEYAQQMAEMQRAQKEMEwqrEIARQKAEMDEKEKQRQVEI---ARQMAER 357
Cdd:TIGR02168  315 ERQLEELEAQLEELESKLDELAEELaELEEKLEELKEELESLEAELE---ELEAELEELESRLEELEEQLetlRSKVAQL 391
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   358 QRQEEELLRQQEVALQEAERQKKERERQKeiarqvvERKKQEEVRRIEKARKKSEMEKKERERQQEIARQHAERQRKEEE 437
Cdd:TIGR02168  392 ELQIASLNNEIERLEARLERLEDRRERLQ-------QEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALE 464
                          250       260
                   ....*....|....*....|....*..
gi 597837628   438 ARRQEEARLFAERQKKERERQEEIARQ 464
Cdd:TIGR02168  465 ELREELEEAEQALDAAERELAQLQARL 491
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
280-424 3.45e-07

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: 52.96  E-value: 3.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 280 QKEREELEwqqEIARQEAERQRKEEE-----MRRQQEYAQQMAEMQRAQKEMEWQREIARQKAEMDEKEKQRqveiarqM 354
Cdd:cd16269  148 LEDREKLV---EKYRQVPRKGVKAEEvlqefLQSKEAEAEAILQADQALTEKEKEIEAERAKAEAAEQERKL-------L 217
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 597837628 355 AERQRQEEELLRQQEVALQEAERQ---KKERERQKEIARQvveRKKQEEVRRIEKARKKSEMEKKERERQQEI 424
Cdd:cd16269  218 EEQQRELEQKLEDQERSYEEHLRQlkeKMEEERENLLKEQ---ERALESKLKEQEALLEEGFKEQAELLQEEI 287
growth_prot_Scy NF041483
polarized growth protein Scy;
264-547 4.06e-05

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 47.51  E-value: 4.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  264 ERQRQQEIARQVAERQQKErEELEWqqeiARQEAERQRKE-----EEMRRQQEYA----QQMAEMQRAQKEMEWQREIAR 334
Cdd:NF041483  505 ERVRTEAIERATTLRRQAE-ETLER----TRAEAERLRAEaeeqaEEVRAAAERAarelREETERAIAARQAEAAEELTR 579
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  335 QKAEMDEK--EKQRQVEIARQMAERQRQE--EELLRQQEVA------LQEAERQKKERERQKEIARQVVERKKQEEVRRI 404
Cdd:NF041483  580 LHTEAEERltAAEEALADARAEAERIRREaaEETERLRTEAaerirtLQAQAEQEAERLRTEAAADASAARAEGENVAVR 659
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  405 EKARKKSEMEKKERERQQEIARQHAERQRKEEEARRQEEARLFAERQKKERERqeeiaRQMEEEEKRQREEAEKEEMRKR 484
Cdd:NF041483  660 LRSEAAAEAERLKSEAQESADRVRAEAAAAAERVGTEAAEALAAAQEEAARRR-----REAEETLGSARAEADQERERAR 734
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 597837628  485 KIEEERLRKEEEQRIEAQRKA-----EEERRIEEQLAAREVENQStVVNPAFGMH------IPGETQAGEHSTD 547
Cdd:NF041483  735 EQSEELLASARKRVEEAQAEAqrlveEADRRATELVSAAEQTAQQ-VRDSVAGLQeqaeeeIAGLRSAAEHAAE 807
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
314-407 5.50e-05

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: 43.73  E-value: 5.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   314 QQMAEMQRAQKEMEwqREIARQKAEMDEKEKQrqveiARQMAERQRQEEELLRQQEVALQEAERQKKERE--RQKEIARQ 391
Cdd:smart00935  11 QESPAGKAAQKQLE--KEFKKRQAELEKLEKE-----LQKLKEKLQKDAATLSEAAREKKEKELQKKVQEfqRKQQKLQQ 83
                           90
                   ....*....|....*.
gi 597837628   392 VVERKKQEEVRRIEKA 407
Cdd:smart00935  84 DLQKRQQEELQKILDK 99
Agg_substance NF033875
LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, ...
96-341 2.29e-04

LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, are LPXTG-anchored large surface proteins that contribute to virulence. Several closely related paralogs may be found in a single strain.


Pssm-ID: 411439 [Multi-domain]  Cd Length: 1306  Bit Score: 45.09  E-value: 2.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   96 PEPTTVRPYRPVFTTPNrKIVSSAATKSPKPPPTRTTATTLTTPPLKNRKVTEPIPVSEAQMTGMQPSTRGYTRGPQMHT 175
Cdd:NF033875   50 PGTTTVQPDNPDPQSGS-ETPKTAVSEEATVQKDTTSQPTKVEEVASEKNGAEQSSATPNDTTNAQQPTVGAEKSAQEQP 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  176 tgVTAGTTSGEHMVNYKGITMSEDEFLKQLVRIVEAHQVAINKieeQVGEERRRGGVEDHEHPAGSFrkqGPSGNFEEGS 255
Cdd:NF033875  129 --VVSPETTNEPLGQPTEVAPAENEANKSTSIPKEFETPDVDK---AVDEAKKDPNITVVEKPAEDL---GNVSSKDLAA 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  256 SNAEMEQLERQRQQEIARQVAERQQKEREELEWQQEI-ARQEAERQRKEEEMRRQQEYAQQMAEMQRA-QKEMEWQREIA 333
Cdd:NF033875  201 KEKEVDQLQKEQAKKIAQQAAELKAKNEKIAKENAEIaAKNKAEKERYEKEVAEYNKHKNENGYVNEAiSKNLVFDQSVV 280

                  ....*...
gi 597837628  334 RQKAEMDE 341
Cdd:NF033875  281 TKDTKISS 288
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
251-581 9.92e-03

pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.


Pssm-ID: 468201 [Multi-domain]  Cd Length: 684  Bit Score: 39.61  E-value: 9.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 251 FEEGSSNAEMEQLERQRQQEIARQVAERQQKER--------------EELEWQQEIARQEAER-QRKEEEMRRQQEYAQQ 315
Cdd:NF033838 130 FKKDTLEPGKKVAEATKKVEEAEKKAKDQKEEDrrnyptntyktlelEIAESDVEVKKAELELvKEEAKEPRDEEKIKQA 209
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 316 MAEMQRAQKEMEWQREIA--RQKAEMDEKEKQ--RQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQ 391
Cdd:NF033838 210 KAKVESKKAEATRLEKIKtdREKAEEEAKRRAdaKLKEAVEKNVATSEQDKPKRRAKRGVLGEPATPDKKENDAKSSDSS 289
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 392 V-----------VERKKQEEVRRIEKARKKSEMEKKERERQ-QEIARQHAERQRKEEEARRQEEARLFAERQKKERERQE 459
Cdd:NF033838 290 VgeetlpspslkPEKKVAEAEKKVEEAKKKAKDQKEEDRRNyPTNTYKTLELEIAESDVKVKEAELELVKEEAKEPRNEE 369
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 460 EIarqmeEEEKRQREEAEKEEMRKRKIEEERLRKEEeqriEAQRK-AEEERRIEEQLAAREVENQSTVVNPAFGMHIPGE 538
Cdd:NF033838 370 KI-----KQAKAKVESKKAEATRLEKIKTDRKKAEE----EAKRKaAEEDKVKEKPAEQPQPAPAPQPEKPAPKPEKPAE 440
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 597837628 539 TQAGEHSTDYYG---YSTNSDATktvlaglmsmSSRLTSTEPPQLE 581
Cdd:NF033838 441 QPKAEKPADQQAeedYARRSEEE----------YNRLTQQQPPKTE 476
 
Name Accession Description Interval E-value
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
39-696 1.06e-43

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: 169.92  E-value: 1.06e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   39 EEFIFSTKRPKRPRPKTKAASStltaaptsaasssthpstttptpTVAFPTPALLPTPEPTTVRPYRPVFTTPNRKIVSS 118
Cdd:pfam17380 101 EEFVFSTIRPKSRKPKARTRGK-----------------------KRKTTTTMIQTTTPMMVTTSSSALEMTTTPKIVIF 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  119 AATKSPKPPPTRTTATTLTTPPLKNRKV------------TEPIPVSEA---------------QMTGMQPSTRGYT--- 168
Cdd:pfam17380 158 ASKKNASGGNRSGEQRKQIQLIRRRRGNhsaftrpgrprtTTPMPVTHAtrfvpgiqmstvapkEVQGMPHTLAPYEkme 237
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  169 RGPQMHTTGVTAGTTSGEHMVNYKGITMSEDEFLKQLVRIVEaHQVAINKIEEQvgeerrrggvEDHEHPAGSFRKQGPS 248
Cdd:pfam17380 238 RRKESFNLAEDVTTMTPEYTVRYNGQTMTENEFLNQLLHIVQ-HQKAVSERQQQ----------EKFEKMEQERLRQEKE 306
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  249 GNFEEGSSNAEMEQLERQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQMAEMqraqkemew 328
Cdd:pfam17380 307 EKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERIRQEEIAMEISRM--------- 377
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  329 qREIARQKAEMDEKEkqrqveiarqmaERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVERKKQEEVRRIEKAR 408
Cdd:pfam17380 378 -RELERLQMERQQKN------------ERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEER 444
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  409 KKsemeKKERERQQEIARQHaERQRKEEEARRQEEARLFAERQKKERERQEEIARQMEEEEKRQREEAEKEEMRKRKIEE 488
Cdd:pfam17380 445 AR----EMERVRLEEQERQQ-QVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLE 519
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  489 ERLRKEEEQRIEAQ--RKAEEERRIEEQLAARE---------VENQSTVVNPAFGMHIPGETQAGEHSTDYYGYSTNSDA 557
Cdd:pfam17380 520 KEMEERQKAIYEEErrREAEEERRKQQEMEERRriqeqmrkaTEERSRLEAMEREREMMRQIVESEKARAEYEATTPITT 599
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  558 TKTVlaglmsMSSRLTSTEPPQLE--IIHFTAPPPtpsspanEWVT-SPHSWRPPPDMQTNVLEWSRTPIpstgtselps 634
Cdd:pfam17380 600 IKPI------YRPRISEYQPPDVEshMIRFTTQSP-------EWATpSPATWNPEWNTVTAEEETPGIPI---------- 656
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 597837628  635 tVTSECDSNVECAFSYEDDLLCPHPNDATRYLQCTPMIGRRGRWTERMCPPNLVFIPSYGRC 696
Cdd:pfam17380 657 -IHSQCQVNGECELKYDSDSFCAHPSNPSMYLQCAPLYGRLGRWTERHCPDTLIFIVSIGRC 717
PTZ00121 PTZ00121
MAEBL; Provisional
252-521 4.45e-23

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 106.38  E-value: 4.45e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  252 EEGSSNAEMEQLERQRQQEIARQVAERQQKErEELEWQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEWQRE 331
Cdd:PTZ00121 1363 EEKAEAAEKKKEEAKKKADAAKKKAEEKKKA-DEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAE 1441
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  332 IARQKAEMDEK-EKQRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQK---EIARQVVERKKQEEVRRIEKA 407
Cdd:PTZ00121 1442 EAKKADEAKKKaEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKkadEAKKAAEAKKKADEAKKAEEA 1521
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  408 RKKSEMEKKERERQQEIARQHAERQR----KEEEARRQEEARLFAERQKKERE------RQEEIARQMEEEEKRQREEAE 477
Cdd:PTZ00121 1522 KKADEAKKAEEAKKADEAKKAEEKKKadelKKAEELKKAEEKKKAEEAKKAEEdknmalRKAEEAKKAEEARIEEVMKLY 1601
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 597837628  478 KEEmRKRKIEEERLRKEEEQRIEAQRKAEEERRIEEQLAAREVE 521
Cdd:PTZ00121 1602 EEE-KKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAE 1644
PTZ00121 PTZ00121
MAEBL; Provisional
252-523 5.68e-22

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 102.91  E-value: 5.68e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  252 EEGSSNAE--MEQLERQRQQEIARQVAERQQKEREELEWQQEiARQEAERQRKEEEMR------RQQEYAQQMAEMQRAQ 323
Cdd:PTZ00121 1394 DEAKKKAEedKKKADELKKAAAAKKKADEAKKKAEEKKKADE-AKKKAEEAKKADEAKkkaeeaKKAEEAKKKAEEAKKA 1472
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  324 KEMEWQREIARQKAEMDEK--EKQRQVEIARQMAERQRQEEELlRQQEVALQEAERQKKERERQKEIARQVVERKKQEEV 401
Cdd:PTZ00121 1473 DEAKKKAEEAKKADEAKKKaeEAKKKADEAKKAAEAKKKADEA-KKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADEL 1551
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  402 RRIEKARKKSEMEKKERERQQEIARQHAERQRKEEEARRQEEARLFAERQKKERERQEEIARQMEEEEKRQREEAEKEEM 481
Cdd:PTZ00121 1552 KKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEE 1631
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 597837628  482 RKRKIEEERLRKEEEQRIEAQRKAEEERRIE-EQLAAREVENQ 523
Cdd:PTZ00121 1632 KKKVEQLKKKEAEEKKKAEELKKAEEENKIKaAEEAKKAEEDK 1674
PTZ00121 PTZ00121
MAEBL; Provisional
198-526 9.84e-21

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 98.67  E-value: 9.84e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  198 EDEFLKQLVRIVEAhqvAINKIEEQVGEERRRGGVED---HEHPAGSFRKQGPSGNFEEGSSNAEMEQLERQRQQEIARQ 274
Cdd:PTZ00121 1221 EDAKKAEAVKKAEE---AKKDAEEAKKAEEERNNEEIrkfEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKK 1297
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  275 VAERQQ-----KEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEWQR-EIARQKAEMDEK---EKQ 345
Cdd:PTZ00121 1298 AEEKKKadeakKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEaEAAEEKAEAAEKkkeEAK 1377
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  346 RQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQvveRKKQEEVRRIEKARKKSEMEKKERErqqeiA 425
Cdd:PTZ00121 1378 KKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEA---KKKAEEKKKADEAKKKAEEAKKADE-----A 1449
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  426 RQHAERQRKEEEARRQEEARLFAERQKK---ERERQEEIARQMEEEEKRQREEAEKEEMRKR----KIEEERLRKEEEQR 498
Cdd:PTZ00121 1450 KKKAEEAKKAEEAKKKAEEAKKADEAKKkaeEAKKADEAKKKAEEAKKKADEAKKAAEAKKKadeaKKAEEAKKADEAKK 1529
                         330       340
                  ....*....|....*....|....*...
gi 597837628  499 IEAQRKAEEERRIEEQLAAREVENQSTV 526
Cdd:PTZ00121 1530 AEEAKKADEAKKAEEKKKADELKKAEEL 1557
PTZ00121 PTZ00121
MAEBL; Provisional
220-523 1.23e-20

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 98.29  E-value: 1.23e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  220 EEQVGEERRRGGVEDHEHPAGSFRKQGPSGNFEEGSSNAEmeqlERQRQQEIARQVAERQQ----KEREELEWQQEIARQ 295
Cdd:PTZ00121 1389 EKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAE----EKKKADEAKKKAEEAKKadeaKKKAEEAKKAEEAKK 1464
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  296 EAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEWQREIARQKAemdekEKQRQVEIARQMAERQRQEEelLRQQEVALQEA 375
Cdd:PTZ00121 1465 KAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAA-----EAKKKADEAKKAEEAKKADE--AKKAEEAKKAD 1537
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  376 ERQKKERERQKEIARQVVERKKQEEVRRIEKARKKSEmEKKERERQQEIARQHAERQRKEEEARRQEEARLFAERQKKER 455
Cdd:PTZ00121 1538 EAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEE-DKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAE 1616
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 597837628  456 E---RQEEIAR-QMEEEEKRQREEAEKEEMRKRKIEEERLRKEEEQRIEAQRKAEEERRIEEQLAAREVENQ 523
Cdd:PTZ00121 1617 EakiKAEELKKaEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEK 1688
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
252-522 1.52e-19

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 94.23  E-value: 1.52e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 252 EEGSSNAEMEQLERQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEwqRE 331
Cdd:COG1196  289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE--EA 366
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 332 IARQKAEMDEKEKQRQvEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVERKKQEEVRRIEKARKKS 411
Cdd:COG1196  367 LLEAEAELAEAEEELE-ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 412 EMEKKERERQQEIARQHAERQRKEEEARRQEearlfAERQKKERERQEEIARQMEEEEKRQREEAEKEEMRKRKIEEERL 491
Cdd:COG1196  446 EAAEEEAELEEEEEALLELLAELLEEAALLE-----AALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLR 520
                        250       260       270
                 ....*....|....*....|....*....|.
gi 597837628 492 RKEEEQRIEAQRKAEEERRIEEQLAAREVEN 522
Cdd:COG1196  521 GLAGAVAVLIGVEAAYEAALEAALAAALQNI 551
PTZ00121 PTZ00121
MAEBL; Provisional
264-521 3.98e-19

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 93.28  E-value: 3.98e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  264 ERQRQQEIARQVAERQQKErEELEWQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEwQREIARQKAEMDEKE 343
Cdd:PTZ00121 1454 EEAKKAEEAKKKAEEAKKA-DEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAK-KAEEAKKADEAKKAE 1531
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  344 KQRQVEIARQmAERQRQEEELLRQQEValQEAERQKKERERQKEIARQVVERKKQEEVRRIEKARKKSEMEKKERERQQ- 422
Cdd:PTZ00121 1532 EAKKADEAKK-AEEKKKADELKKAEEL--KKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMk 1608
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  423 -EIARQHAERQRKEEEARRQEEARLFAERQKK----ERERQEEIARQMEEEEKRQREEAEKEEMRKRKIEE-ERLRKEEE 496
Cdd:PTZ00121 1609 aEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKkeaeEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEaKKAEEDEK 1688
                         250       260
                  ....*....|....*....|....*
gi 597837628  497 QRIEAQRKAEEERRIEEQLAAREVE 521
Cdd:PTZ00121 1689 KAAEALKKEAEEAKKAEELKKKEAE 1713
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
265-521 6.23e-19

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 92.31  E-value: 6.23e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 265 RQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRR-QQEYAQQMAEMQRAQKEMEwqrEIARQKAEMDEKE 343
Cdd:COG1196  235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEElELELEEAQAEEYELLAELA---RLEQDIARLEERR 311
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 344 KQRQVEIARQMAERQRQEEELLRQQEvALQEAERQKKERERQKEIARQVVERKKQEEVRRIEKARKKSEMEKKERERQQE 423
Cdd:COG1196  312 RELEERLEELEEELAELEEELEELEE-ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 424 IARQHAERQRKEEEARRQEEARLfAERQKKERERQEEIARQMEEEEKRQREEAEKEEMRKRKIEEERLRKEEEQRIEAQR 503
Cdd:COG1196  391 ALRAAAELAAQLEELEEAEEALL-ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
                        250
                 ....*....|....*...
gi 597837628 504 KAEEERRIEEQLAAREVE 521
Cdd:COG1196  470 EEAALLEAALAELLEELA 487
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
257-524 3.20e-18

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 90.00  E-value: 3.20e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 257 NAEMEQLERQRQQEIARQvaERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEWQREIARQK 336
Cdd:COG1196  245 EAELEELEAELEELEAEL--AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELE 322
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 337 AEMDEKEKQRQvEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVERKKQEEVRRIEKARKKSEMEKK 416
Cdd:COG1196  323 EELAELEEELE-ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 417 ERERQQEIARQHAERQRKEEEARRQEEARLFAERQKKERERQEEIARQMEEEEKRQREEAEKEEMRKRKIEEERLRKEEE 496
Cdd:COG1196  402 LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
                        250       260
                 ....*....|....*....|....*...
gi 597837628 497 QRIEAQRKAEEERRIEEQLAAREVENQS 524
Cdd:COG1196  482 LLEELAEAAARLLLLLEAEADYEGFLEG 509
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
260-523 5.77e-18

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 89.23  E-value: 5.77e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 260 MEQLERQRQQ--------------EIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMR-RQQEYAQQMAEMQRAQK 324
Cdd:COG1196  202 LEPLERQAEKaeryrelkeelkelEAELLLLKLRELEAELEELEAELEELEAELEELEAELAeLEAELEELRLELEELEL 281
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 325 EMEW-QREIARQKAEMDEKEKQRQVEIARQmAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVERKKQEEVRR 403
Cdd:COG1196  282 ELEEaQAEEYELLAELARLEQDIARLEERR-RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 404 IEKARKKSEMEKKERERQQEIARQHAERQRKEEEARRQEEARLFAERQkkERERQEEIARQMEEEEKRQREEAEKEEMRK 483
Cdd:COG1196  361 AEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA--EEALLERLERLEEELEELEEALAELEEEEE 438
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 597837628 484 RKIEEERLRKEEEQRIEAQRKAEEERRIEEQLAAREVENQ 523
Cdd:COG1196  439 EEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
258-521 7.78e-18

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 88.84  E-value: 7.78e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 258 AEMEQLERQR---QQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEM-RRQQEYAQQMAEMQRAQKEMEWQREIA 333
Cdd:COG1196  232 LKLRELEAELeelEAELEELEAELEELEAELAELEAELEELRLELEELELELeEAQAEEYELLAELARLEQDIARLEERR 311
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 334 RQKAEMDEKEKQRQVEIARQMAERQRQEEELLRQQEvALQEAERQKKERERQKEIARQVVERKKQEEVRRIEKARKksem 413
Cdd:COG1196  312 RELEERLEELEEELAELEEELEELEEELEELEEELE-EAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE---- 386
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 414 EKKERERQQEIARQHAERQRKEEEARRQEEARLFAERQKKERERQEEIARQMEEEEKRQREEAEKEEMRKRKIEEERLRK 493
Cdd:COG1196  387 ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
                        250       260
                 ....*....|....*....|....*...
gi 597837628 494 EEEQRIEAQRKAEEERRIEEQLAAREVE 521
Cdd:COG1196  467 ELLEEAALLEAALAELLEELAEAAARLL 494
PTZ00121 PTZ00121
MAEBL; Provisional
210-513 1.63e-17

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 88.27  E-value: 1.63e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  210 EAHQVAINKIEEQVGEERRRGGVEDhehpagsFRKQGPSGNFEEGSSNAEMEQLERQRQQEIARQV--AERQQKEREELE 287
Cdd:PTZ00121 1102 EAKKTETGKAEEARKAEEAKKKAED-------ARKAEEARKAEDARKAEEARKAEDAKRVEIARKAedARKAEEARKAED 1174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  288 WQQEIARQEAERQRKEEEMRRQQEyAQQMAEMQRAqkEMEWQREIARQKAEMDEKEKQRQVEIARQMAERQRQEEELLRQ 367
Cdd:PTZ00121 1175 AKKAEAARKAEEVRKAEELRKAED-ARKAEAARKA--EEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNN 1251
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  368 QEVALQEAERQKKERERQKEIARQvvERKKQEEVRRIEKARKKSEMEKKERERQQEIARQHAE-RQRKEEEARRQEEARL 446
Cdd:PTZ00121 1252 EEIRKFEEARMAHFARRQAAIKAE--EARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEeAKKADEAKKKAEEAKK 1329
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 597837628  447 FAERQKKERERQEEIARQMEEEEKRQREEAEKEEmRKRKIEEERLRKEEEQRIEAQRKAEEERRIEE 513
Cdd:PTZ00121 1330 KADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAE-EKAEAAEKKKEEAKKKADAAKKKAEEKKKADE 1395
PTZ00121 PTZ00121
MAEBL; Provisional
206-514 1.98e-17

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 87.89  E-value: 1.98e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  206 VRIVEAHQVAIN--KIEE--QVGEERRRGGVEDHEHPAgsfRKQGPSGNFEEGSSNAEMEQLERQRQQEIAR-QVAERQQ 280
Cdd:PTZ00121 1199 ARKAEAARKAEEerKAEEarKAEDAKKAEAVKKAEEAK---KDAEEAKKAEEERNNEEIRKFEEARMAHFARrQAAIKAE 1275
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  281 KEREELEWQQEIARQEAERQRKEEEMRRQQEyAQQMAEMQRAQKEMEWQREIARQKAEmdekEKQRQVEIARQMAERQRQ 360
Cdd:PTZ00121 1276 EARKADELKKAEEKKKADEAKKAEEKKKADE-AKKKAEEAKKADEAKKKAEEAKKKAD----AAKKKAEEAKKAAEAAKA 1350
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  361 EEELLRQQevaLQEAERQKKERERQKEIARQVVE--RKKQEEVRRIEKARKKSEMEKKERE--RQQEIARQHAER-QRKE 435
Cdd:PTZ00121 1351 EAEAAADE---AEAAEEKAEAAEKKKEEAKKKADaaKKKAEEKKKADEAKKKAEEDKKKADelKKAAAAKKKADEaKKKA 1427
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  436 EEARRQEEARLFAERQKK--ERERQEEIARQMEEEEKRQREEAEKEEMRKRKIEEERLRKEEEQRIEAQRKAEEERRIEE 513
Cdd:PTZ00121 1428 EEKKKADEAKKKAEEAKKadEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAE 1507

                  .
gi 597837628  514 Q 514
Cdd:PTZ00121 1508 A 1508
PTZ00121 PTZ00121
MAEBL; Provisional
218-514 4.97e-17

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 86.73  E-value: 4.97e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  218 KIEEQVGEERRRGGVEDHEHPAGSFRKQGpsgnfEEGSSNAEMEQLERQRQQEIARQVAERqqKEREELEWQQEIarQEA 297
Cdd:PTZ00121 1478 KAEEAKKADEAKKKAEEAKKKADEAKKAA-----EAKKKADEAKKAEEAKKADEAKKAEEA--KKADEAKKAEEK--KKA 1548
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  298 ERQRKEEEMRRqqeyAQQMAEMQRAQKEMEWQREIARQKAEMDEKEKQRQVEIARQMAERQRQEEELLRQQEVALQEAER 377
Cdd:PTZ00121 1549 DELKKAEELKK----AEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEE 1624
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  378 QKKERERQKEIARqvVERKKQEEVRRIEKARKKSE---MEKKERERQQEIARQHAERQRKEEEARRQEEARLfaERQKKE 454
Cdd:PTZ00121 1625 LKKAEEEKKKVEQ--LKKKEAEEKKKAEELKKAEEenkIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEAL--KKEAEE 1700
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  455 RERQEEIARQMEEEEKRQREEAEKEEMRKRKIEEErlRKEEEqriEAQRKAEEERRIEEQ 514
Cdd:PTZ00121 1701 AKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEA--KKEAE---EDKKKAEEAKKDEEE 1755
PTZ00121 PTZ00121
MAEBL; Provisional
218-521 6.92e-17

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 85.96  E-value: 6.92e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  218 KIEEQVGEERRRGGVEDHEHPAGSFRKQGPSGNFEEGSSNAEmeqlERQRQQEIARQVAErQQKEREELEWQQEIARQE- 296
Cdd:PTZ00121 1452 KAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAE----EAKKKADEAKKAAE-AKKKADEAKKAEEAKKADe 1526
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  297 ---AERQRKEEEMRRQQEY--AQQMAEMQRAQKEMEWQREIARQKAEMDEKEKQRQVEIARQmAERQRQEEELLRQQEVA 371
Cdd:PTZ00121 1527 akkAEEAKKADEAKKAEEKkkADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKK-AEEARIEEVMKLYEEEK 1605
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  372 LQEAERQKKERErqkeiarqvvERKKQEEVRRIEKARKKSEMEKKERERQQEIARQ-----HAERQRKEEEARRQEEARL 446
Cdd:PTZ00121 1606 KMKAEEAKKAEE----------AKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEElkkaeEENKIKAAEEAKKAEEDKK 1675
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  447 FAERQKKERERQEEIARQMEEEEKRQR-----EEAEKEEMRKRKIEEERLRKEEEQRIEAQRKAEEERRIEEQLAAREVE 521
Cdd:PTZ00121 1676 KAEEAKKAEEDEKKAAEALKKEAEEAKkaeelKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE 1755
PTZ00121 PTZ00121
MAEBL; Provisional
216-454 9.47e-17

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 85.58  E-value: 9.47e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  216 INKIEEQVGEERRRGGVEDHEHPAgsfrKQGPSGNFEEGSSNAEMEQL---ERQRQQEIARQVAERQQKEREELEWQQEI 292
Cdd:PTZ00121 1563 KKKAEEAKKAEEDKNMALRKAEEA----KKAEEARIEEVMKLYEEEKKmkaEEAKKAEEAKIKAEELKKAEEEKKKVEQL 1638
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  293 ARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEWQREIARQKAEMDEKEKQRQVeiaRQMAERQRQEEELLRQQEVAL 372
Cdd:PTZ00121 1639 KKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEAL---KKEAEEAKKAEELKKKEAEEK 1715
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  373 QEAERQKKERERQKEIARQVV-----ERKKQEEVRRIEKARKKSEMEKKERERQQEIARQHAERQRKEEEARRQEEARLF 447
Cdd:PTZ00121 1716 KKAEELKKAEEENKIKAEEAKkeaeeDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRME 1795

                  ....*..
gi 597837628  448 AERQKKE 454
Cdd:PTZ00121 1796 VDKKIKD 1802
PTZ00121 PTZ00121
MAEBL; Provisional
240-513 1.13e-16

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 85.58  E-value: 1.13e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  240 GSFRKQGPSgnfeegSSNAEMEQLERQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEyAQQMAEM 319
Cdd:PTZ00121 1067 GQDEGLKPS------YKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEE-ARKAEDA 1139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  320 QRAQKemewqreiARQKAEMDEKEKQRQVEIARQMAERQRQEEEllRQQEVALQEAERQKKERERQKEIARQVVERKKQE 399
Cdd:PTZ00121 1140 RKAEE--------ARKAEDAKRVEIARKAEDARKAEEARKAEDA--KKAEAARKAEEVRKAEELRKAEDARKAEAARKAE 1209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  400 EVRRIEKARKKSEMEKKERERQQEIARQHAErqrkeeEARRQEEARLFAERQKKERERQEEIARQmeEEEKRQREEAEKE 479
Cdd:PTZ00121 1210 EERKAEEARKAEDAKKAEAVKKAEEAKKDAE------EAKKAEEERNNEEIRKFEEARMAHFARR--QAAIKAEEARKAD 1281
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 597837628  480 EMRK----RKIEEERLRKEEEQRIEAQRKAEEERRIEE 513
Cdd:PTZ00121 1282 ELKKaeekKKADEAKKAEEKKKADEAKKKAEEAKKADE 1319
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
274-419 2.01e-16

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 82.61  E-value: 2.01e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 274 QVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYAqqMAEMQRAQKEMEWQREIARQKAEMDEKEKQRQVEIARQ 353
Cdd:COG2268  196 EIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREIE--TARIAEAEAELAKKKAEERREAETARAEAEAAYEIAEA 273
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 597837628 354 MAER--QRQEEELLRQQEVALQEAERQKKERERQKEIARQVVERKKQEEVRriEKARKKSEMEKKERE 419
Cdd:COG2268  274 NAERevQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAE--AEAEAEAIRAKGLAE 339
PTZ00121 PTZ00121
MAEBL; Provisional
252-523 2.62e-16

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 84.42  E-value: 2.62e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  252 EEGSSNAEMEQLERQRQQEIARQVAERqqKEREELEWQQEIARQE----AERQRKEEEMR----RQQEYAQQmAEMQRAQ 323
Cdd:PTZ00121 1519 EEAKKADEAKKAEEAKKADEAKKAEEK--KKADELKKAEELKKAEekkkAEEAKKAEEDKnmalRKAEEAKK-AEEARIE 1595
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  324 KEMEWQREIARQKAEMDEKEKQRQV--EIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKeIARQVVERKKQEEV 401
Cdd:PTZ00121 1596 EVMKLYEEEKKMKAEEAKKAEEAKIkaEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENK-IKAAEEAKKAEEDK 1674
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  402 RRIEKARKKSEMEKKERE---RQQEIARQHAERQRKEEEARRQeearlfAERQKKERERQE---EIARQMEEEEKRQREE 475
Cdd:PTZ00121 1675 KKAEEAKKAEEDEKKAAEalkKEAEEAKKAEELKKKEAEEKKK------AEELKKAEEENKikaEEAKKEAEEDKKKAEE 1748
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 597837628  476 AEKEEMRKRKIEEERLrkeeeqriEAQRKAEEERRIEEQLAAREVENQ 523
Cdd:PTZ00121 1749 AKKDEEEKKKIAHLKK--------EEEKKAEEIRKEKEAVIEEELDEE 1788
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
261-519 3.64e-14

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: 74.57  E-value: 3.64e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  261 EQLERQRQQEIARQVAERQQKEREELEWQQEIARQEA-ERQRKEEEMRRQQEYAQQMAEMQRAQKEMewQREIARQKAEM 339
Cdd:pfam13868  26 AQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEkEEERKEERKRYRQELEEQIEEREQKRQEE--YEEKLQEREQM 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  340 DEKEKQRQVEIARQMAERQRQEEELLRQQEVALQEAERQK-KERERQKEIARQVVERKKQEEVRRIEKARKKSEMEKKER 418
Cdd:pfam13868 104 DEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKeLEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKE 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  419 ERQQEIARQHAERQRKEEEARRQEEARLFAERQKKERERQEEIARQMEEEEKRQREEAEKEEMRKRKIEEERLRKEEEQR 498
Cdd:pfam13868 184 REIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEF 263
                         250       260
                  ....*....|....*....|.
gi 597837628  499 IEAQRKAEEERRIEEQLAARE 519
Cdd:pfam13868 264 ERMLRKQAEDEEIEQEEAEKR 284
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
261-523 7.81e-14

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: 73.80  E-value: 7.81e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  261 EQLERQRQQEIARQVAERQQKEREELEWQQEIARQ----EAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEWQREIARQK 336
Cdd:pfam13868  47 EMMEEERERALEEEEEKEEERKEERKRYRQELEEQieerEQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQR 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  337 AEMDEKEKQRQVEIARQMAERQRQEEELLRqqevaLQEAERQKKERERQKEIARQVVERKKQEEVRRIEKARKKSEMEKK 416
Cdd:pfam13868 127 QLREEIDEFNEEQAEWKELEKEEEREEDER-----ILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKA 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  417 ERER------QQEIARQHAERQRKEEEARRQEEARLFAERQKKERERQEEIARQMEEEEKrqreeaEKEEMRKRKieeer 490
Cdd:pfam13868 202 ERDElraklyQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEE------EFERMLRKQ----- 270
                         250       260       270
                  ....*....|....*....|....*....|...
gi 597837628  491 lrkeeEQRIEAQRKAEEERRIEEQLAAREVENQ 523
Cdd:pfam13868 271 -----AEDEEIEQEEAEKRRMKRLEHRRELEKQ 298
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
258-513 2.05e-13

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: 72.64  E-value: 2.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  258 AEMEQLERQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQMAE---MQRAQKEMEWQREIAR 334
Cdd:pfam13868  93 YEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEderILEYLKEKAEREEERE 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  335 QKAEMDEKEKQRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIArqvveRKKQEEVRRIEKARKKsEME 414
Cdd:pfam13868 173 AEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEA-----EKKARQRQELQQAREE-QIE 246
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  415 KKERERQQEIARQHAERQR--KEEEARRQEEARLFAERQKKERERQEEIARQMeeeekrqreeAEKEEMRKRKIEEERLR 492
Cdd:pfam13868 247 LKERRLAEEAEREEEEFERmlRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQI----------EEREEQRAAEREEELEE 316
                         250       260
                  ....*....|....*....|.
gi 597837628  493 KEEeqriEAQRKAEEERRIEE 513
Cdd:pfam13868 317 GER----LREEEAERRERIEE 333
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
256-430 1.23e-12

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 70.61  E-value: 1.23e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 256 SNAEMEQLERQRQQEIARQVAERQQKEREELEWQQEIARQEAERQR-KEEEMRRQQEyaqqmaemQRAQKEMEWQREIAR 334
Cdd:PRK09510  57 PGAVVEQYNRQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERlKQLEKERLAA--------QEQKKQAEEAAKQAA 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 335 QKAEMDEKEKQRQVEIARQMAERQRQEEELLRQQevalQEAERQKKERERQKeiARQVVERKKQEEVRRIEK----ARKK 410
Cdd:PRK09510 129 LKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKK----AAAEAKKKAEAEAA--KKAAAEAKKKAEAEAAAKaaaeAKKK 202
                        170       180
                 ....*....|....*....|
gi 597837628 411 SEMEKKERERQQEIARQHAE 430
Cdd:PRK09510 203 AEAEAKKKAAAEAKKKAAAE 222
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
202-464 8.20e-12

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: 69.32  E-value: 8.20e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   202 LKQLVRIVEAHQVAINKIEEQVgEERRRGGVEDHEhpagsfRKQGPSGNFEEgsSNAEMEQLErqrqQEIARQVAERQQK 281
Cdd:TIGR02168  248 LKEAEEELEELTAELQELEEKL-EELRLEVSELEE------EIEELQKELYA--LANEISRLE----QQKQILRERLANL 314
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   282 EREELEWQQEIARQEAERQRKEEEM-RRQQEYAQQMAEMQRAQKEMEwqrEIARQKAEMDEKEKQRQVEI---ARQMAER 357
Cdd:TIGR02168  315 ERQLEELEAQLEELESKLDELAEELaELEEKLEELKEELESLEAELE---ELEAELEELESRLEELEEQLetlRSKVAQL 391
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   358 QRQEEELLRQQEVALQEAERQKKERERQKeiarqvvERKKQEEVRRIEKARKKSEMEKKERERQQEIARQHAERQRKEEE 437
Cdd:TIGR02168  392 ELQIASLNNEIERLEARLERLEDRRERLQ-------QEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALE 464
                          250       260
                   ....*....|....*....|....*..
gi 597837628   438 ARRQEEARLFAERQKKERERQEEIARQ 464
Cdd:TIGR02168  465 ELREELEEAEQALDAAERELAQLQARL 491
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
258-465 1.34e-11

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: 66.87  E-value: 1.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  258 AEMEQLERQRQQEIARQVAERQ-QKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQMaemQRAQKEMEWQREIARQK 336
Cdd:pfam13868 140 AEWKELEKEEEREEDERILEYLkEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDE---KAERDELRAKLYQEEQE 216
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  337 AEMDEKEKQrqveiarQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVERKKQEEVRRIEKARKKSEMEKK 416
Cdd:pfam13868 217 RKERQKERE-------EAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRL 289
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 597837628  417 ERERQQEIARQHAERQRKEEEARRQEEARLFAERQKKERERQEEIARQM 465
Cdd:pfam13868 290 EHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKK 338
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
250-464 2.70e-11

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: 67.77  E-value: 2.70e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   250 NFEEGSSNAEMEQLERQ---RQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEyaqQMAEMQRAQKEM 326
Cdd:TIGR02168  245 QEELKEAEEELEELTAElqeLEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRE---RLANLERQLEEL 321
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   327 EWQREIARQKAEMDEKEKQRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQ-VVERKKQEEV--RR 403
Cdd:TIGR02168  322 EAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSkVAQLELQIASlnNE 401
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 597837628   404 IEKARKKSEMEKKERERQQEIARQHAERQRKEEEARRQEEARLFAERQKKERERQEEIARQ 464
Cdd:TIGR02168  402 IERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEA 462
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
263-432 4.31e-11

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: 66.51  E-value: 4.31e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  263 LERQRQQEIARQV--AERQQKEREELEW----QQEIARQEAERQRKEEEMRRQQEYAQQ-MAEMQRAQKEmewQREIARQ 335
Cdd:pfam15709 325 LEKREQEKASRDRlrAERAEMRRLEVERkrreQEEQRRLQQEQLERAEKMREELELEQQrRFEEIRLRKQ---RLEEERQ 401
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  336 KAEMDEKEKQRQVEIARQMAERQRQE---EELLRQQEVALQEAERQKKERERQKEIARQVVERKKQ----EEVRRIEKAR 408
Cdd:pfam15709 402 RQEEEERKQRLQLQAAQERARQQQEEfrrKLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRlmemAEEERLEYQR 481
                         170       180
                  ....*....|....*....|....
gi 597837628  409 KKSEMEKKERERQQEiARQHAERQ 432
Cdd:pfam15709 482 QKQEAEEKARLEAEE-RRQKEEEA 504
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
304-432 8.79e-11

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 64.83  E-value: 8.79e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 304 EEMRRQQeyaQQMAEMQRAQKEMEWQRE-IARQKAEMDEKEKQRQVEIARQMAERQRQEEellrQQEVALQEAERQKKER 382
Cdd:PRK09510  62 EQYNRQQ---QQQKSAKRAEEQRKKKEQqQAEELQQKQAAEQERLKQLEKERLAAQEQKK----QAEEAAKQAALKQKQA 134
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 597837628 383 ERQKEIARQVVERKKQEEVRRIEKARKKSEMEKKERERQQEIARQHAERQ 432
Cdd:PRK09510 135 EEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAK 184
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
258-523 8.79e-11

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: 65.85  E-value: 8.79e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   258 AEME-QLER-QRQQEIARQVAErQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEWQREIAR- 334
Cdd:TIGR02168  196 NELErQLKSlERQAEKAERYKE-LKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRl 274
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   335 QKAEMDEKEKQRQ-------VEIAR--QMAERQRQEEELLRQQEVALQEA-ERQKKERERQKEIARQVVERKK--QEEVR 402
Cdd:TIGR02168  275 EVSELEEEIEELQkelyalaNEISRleQQKQILRERLANLERQLEELEAQlEELESKLDELAEELAELEEKLEelKEELE 354
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   403 RIEKARKKSEMEKKERERQQEIARQHAERQRKEEEARRQEEARLFAERQ---------KKERERQEEIARQMEEEEKRQR 473
Cdd:TIGR02168  355 SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIErlearlerlEDRRERLQQEIEELLKKLEEAE 434
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 597837628   474 EEAEKEEMRKRKIEEERLRKEEEQRIEAQRKAEEERRIEEQ--LAAREVENQ 523
Cdd:TIGR02168  435 LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQalDAAERELAQ 486
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
329-456 9.73e-11

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 64.89  E-value: 9.73e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 329 QREIARQKAEMDEKEKQRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVERKKQE-----EVRR 403
Cdd:COG2268  193 KIAEIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETARAEaeaayEIAE 272
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 597837628 404 IEkARKKSEMEKKERERQQEIARQHAERQRKEEEARRQEEARLFAERQKKERE 456
Cdd:COG2268  273 AN-AEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAE 324
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
307-432 1.10e-10

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 64.89  E-value: 1.10e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 307 RRQQEYAQQMAEMQRAQKEMEWQREIARQKAEMDEKEKQRQVEIA-RQMAERQRqeeELLRQQEVALQEAERQKKERERQ 385
Cdd:COG2268  191 RRKIAEIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREIEtARIAEAEA---ELAKKKAEERREAETARAEAEAA 267
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 597837628 386 KEIARQVVER--KKQEEVRRIEKARKKSEMEKKERERQQE---IARQHAERQ 432
Cdd:COG2268  268 YEIAEANAERevQRQLEIAEREREIELQEKEAEREEAELEadvRKPAEAEKQ 319
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
251-516 1.30e-10

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: 65.38  E-value: 1.30e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   251 FEEGSSNAEMEQLERQRQQEIARQVAERQQKEREELEWQ---QEIARQEAERQRKEEEM---RRQQEYAQQMAEMQRAQK 324
Cdd:pfam02463  158 IEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKlqeLKLKEQAKKALEYYQLKeklELEEEYLLYLDYLKLNEE 237
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   325 EMEWQREIARQKAEMDEKEKQRQVEIARQMAERQRQEEELLRQQEV-----ALQEAERQKKERERQKEIARQVVERKK-- 397
Cdd:pfam02463  238 RIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLqeeelKLLAKEEEELKSELLKLERRKVDDEEKlk 317
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   398 --QEEVRRIEKARKKS-------EMEKKERERQQEiARQHAERQRKEEEARRQEEARLFAERQKKERERQEEIARQMEEE 468
Cdd:pfam02463  318 esEKEKKKAEKELKKEkeeieelEKELKELEIKRE-AEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEE 396
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 597837628   469 EKRQREEAEKEEMRKRKIEEERLRKEEEQRIEAQRKAEEERRIEEQLA 516
Cdd:pfam02463  397 LELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQG 444
RIB43A pfam05914
RIB43A; This family consists of several RIB43A-like eukaryotic proteins. Ciliary and flagellar ...
260-432 2.18e-10

RIB43A; This family consists of several RIB43A-like eukaryotic proteins. Ciliary and flagellar microtubules contain a specialized set of protofilaments, termed ribbons, that are composed of tubulin and several associated proteins. RIB43A was first characterized in the unicellular biflagellate, Chlamydomonas reinhardtii although highly related sequences are present in several higher eukaryotes including humans. The function of this protein is unknown although the structure of RIB43A and its association with the specialized protofilament ribbons and with basal bodies is relevant to the proposed role of ribbons in forming and stabilising doublet and triplet microtubules and in organizing their three-dimensional structure. Human RIB43A homologs could represent a structural requirement in centriole replication in dividing cells.


Pssm-ID: 461780 [Multi-domain]  Cd Length: 372  Bit Score: 63.38  E-value: 2.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  260 MEQLERQRQQEIA-RQVAERQQKEREELEWQQEIARQE--AERQRKEEEMRRQ-----QEYAQQMAEMQRAQKEMEWQRE 331
Cdd:pfam05914 150 QEQMREWLEQQIEeKKQAEEEEKHAELLYDQKRLERDRraLELAKLEEECRRAvnaatKNFNQALAAEQAERRRLEKRQE 229
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  332 iarQKAEMDEKEKQ---------RQVEIARQMAER----------QRQEEELLRQQEVALQEAERQKK-ERERQKEIARQ 391
Cdd:pfam05914 230 ---QEDNLAEIYNHltsdlltenPEVAQSSLGPHRvipdrwkgmsPEQLKEIRKEQEQQREEKERRREeEKQRDAEWDRQ 306
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 597837628  392 VVERKKQEEVRRIEKARKKSEMEKKERERQQEIARQHAERQ 432
Cdd:pfam05914 307 RLELARAALLLEREQQRLRRELRRQLDEENLQLAQEQKARQ 347
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
258-432 3.85e-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: 63.43  E-value: 3.85e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  258 AEMEQLE----RQRQQEIARQVAERQQKE---REELEWQQEIARQEAE--RQRKEEEMRRQQEY-AQQMAEMQRAQKEME 327
Cdd:pfam15709 343 AEMRRLEverkRREQEEQRRLQQEQLERAekmREELELEQQRRFEEIRlrKQRLEEERQRQEEEeRKQRLQLQAAQERAR 422
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  328 WQREIARQKAEmdekEKQRQveiaRQMAERQRQEEELLRQQEVALQEAERQKKERERQKEiARQVVERKKQEEVrriEKA 407
Cdd:pfam15709 423 QQQEEFRRKLQ----ELQRK----KQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEE-ERLEYQRQKQEAE---EKA 490
                         170       180
                  ....*....|....*....|....*
gi 597837628  408 RKKSEMEKKERERQQEIARQHAERQ 432
Cdd:pfam15709 491 RLEAEERRQKEEEAARLALEEAMKQ 515
PTZ00121 PTZ00121
MAEBL; Provisional
198-401 4.04e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 64.01  E-value: 4.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  198 EDEFLKQLVRIVEAHQVAINKIEEQVGEERRRGGVEDHEHPAGSFRKQGPSGNFEEGSSNAEmeqlERQRQQEIARQVAE 277
Cdd:PTZ00121 1617 EAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAE----EAKKAEEDEKKAAE 1692
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  278 RQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEwqreiaRQKAEMDEKEKQRQVEIARQMAER 357
Cdd:PTZ00121 1693 ALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEED------KKKAEEAKKDEEEKKKIAHLKKEE 1766
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 597837628  358 QRQEEELLRQQEVALQEaERQKKERERQKEIARQVVERKKQEEV 401
Cdd:PTZ00121 1767 EKKAEEIRKEKEAVIEE-ELDEEDEKRRMEVDKKIKDIFDNFAN 1809
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
261-426 8.37e-10

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


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 61.40  E-value: 8.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  261 EQLERQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRK--EEEMRRQQEYAQQMAEMQRAQKEMEWQREIARQKAE 338
Cdd:TIGR02794  78 EEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKqaEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAK 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  339 MDEKE--KQRQVEIARQM---------AERQRQEEELLRQQEVALQ--EAERQKKERERQKEIARQVVERKKQE-EVRRI 404
Cdd:TIGR02794 158 AKAAAeaKKKAEEAKKKAeaeakakaeAEAKAKAEEAKAKAEAAKAkaAAEAAAKAEAEAAAAAAAEAERKADEaELGDI 237
                         170       180
                  ....*....|....*....|..
gi 597837628  405 EKARKKSEMEKKERERQQEIAR 426
Cdd:TIGR02794 238 FGLASGSNAEKQGGARGAAAGS 259
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
240-539 9.98e-10

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: 62.39  E-value: 9.98e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   240 GSFRKQGPSGNF-----EEGSSNAEMEQLERQR---QQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQE 311
Cdd:TIGR02169  658 GSRAPRGGILFSrsepaELQRLRERLEGLKRELsslQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKE 737
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   312 yaqQMAEMQRAQKEMEwqREIARQKAEMDEKEKqrqvEIARQmaerqrqeEELLRQQEVALQEAERqKKERERQKEIARQ 391
Cdd:TIGR02169  738 ---RLEELEEDLSSLE--QEIENVKSELKELEA----RIEEL--------EEDLHKLEEALNDLEA-RLSHSRIPEIQAE 799
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   392 VveRKKQEEVRRIEKARKKSEMEKKERERQQEIA---RQHAERQRKEEEARRQEEARLFAERQKKERERQEEIARQMEEE 468
Cdd:TIGR02169  800 L--SKLEEEVSRIEARLREIEQKLNRLTLEKEYLekeIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAAL 877
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 597837628   469 EKRQREEAEKEEMRKRKIEEERLRKEEEQRIEAQRKAEEER--RIEEQLAAREVENQSTVVNPAFGMHIPGET 539
Cdd:TIGR02169  878 RDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRlsELKAKLEALEEELSEIEDPKGEDEEIPEEE 950
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
258-518 1.21e-09

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: 62.38  E-value: 1.21e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   258 AEMEQLERQ-RQQEIARQVAERQQKEREEL------EWQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEWQR 330
Cdd:TIGR02168  684 EKIEELEEKiAELEKALAELRKELEELEEEleqlrkELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEI 763
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   331 EIARQK-AEMDEKEKQRQVEIARQMAERQRQEEEL--LRQQEVALQEAERQKKERERQKEIARQVVERKKQEEVRRIEKA 407
Cdd:TIGR02168  764 EELEERlEEAEEELAEAEAEIEELEAQIEQLKEELkaLREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDL 843
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   408 RKKSEmekKERERQQEIARQHAERQRKEEEARRQeearlfAERQKKERERQEEIARQMEEEEKRQREEAEKEEMRKRKIE 487
Cdd:TIGR02168  844 EEQIE---ELSEDIESLAAEIEELEELIEELESE------LEALLNERASLEEALALLRSELEELSEELRELESKRSELR 914
                          250       260       270
                   ....*....|....*....|....*....|....
gi 597837628   488 EERLRKEEEQRIEAQRKAE---EERRIEEQLAAR 518
Cdd:TIGR02168  915 RELEELREKLAQLELRLEGlevRIDNLQERLSEE 948
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
261-378 1.35e-09

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


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 57.74  E-value: 1.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  261 EQLERQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEWQREIARQKAEMD 340
Cdd:pfam05672  25 EQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRKAEEEAEEREQREQEEQERLQKQKE 104
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 597837628  341 EKEKQrqveiARQMAERQRQEEELLRQQEvalqEAERQ 378
Cdd:pfam05672 105 EAEAK-----AREEAERQRQEREKIMQQE----EQERL 133
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
252-430 2.42e-09

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: 60.16  E-value: 2.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 252 EEGSSNAEMEQLERQ---RQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQM------------ 316
Cdd:COG4942   49 EEKALLKQLAALERRiaaLARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLgrqpplalllsp 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 317 AEMQRAQKEMEWQREIARQKAEMDEKEKQRQVEIA--RQMAERQRQE-EELLRQQEVALQEAERQKKERErqkEIARQVV 393
Cdd:COG4942  129 EDFLDAVRRLQYLKYLAPARREQAEELRADLAELAalRAELEAERAElEALLAELEEERAALEALKAERQ---KLLARLE 205
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 597837628 394 ERKKQEEVRRIEKARKKSEMEKKERERQQEIARQHAE 430
Cdd:COG4942  206 KELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
PTZ00121 PTZ00121
MAEBL; Provisional
304-520 3.14e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 61.31  E-value: 3.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  304 EEMRRQQEYAQQMAEMQRAQKEMEWQREIARQKAE-MDEKEKQRQVEIARQmAERQRQEEELLRQQEVALQEAERqKKER 382
Cdd:PTZ00121 1085 EDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEaKKKAEDARKAEEARK-AEDARKAEEARKAEDAKRVEIAR-KAED 1162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  383 ERQKEIARQVVERKKQEEVRRIEKARKKSEMEKKERERQQEIARQHAErqrkeeearrqeearlfaERQKKERERQEEIA 462
Cdd:PTZ00121 1163 ARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEE------------------ERKAEEARKAEDAK 1224
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 597837628  463 RqmeeeekrqreeaeKEEMRKrkieeerlrkeeeqrIEAQRKAEEE-RRIEEQLAAREV 520
Cdd:PTZ00121 1225 K--------------AEAVKK---------------AEEAKKDAEEaKKAEEERNNEEI 1254
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
268-525 3.31e-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: 59.47  E-value: 3.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  268 QQEIARQVAERQQKEreelewqQEIARQEAERQRKEEEMRRQQEyAQQMAEMQRaqkemewQREIARQKAemDEKEKQRQ 347
Cdd:TIGR02794  45 PGAVAQQANRIQQQK-------KPAAKKEQERQKKLEQQAEEAE-KQRAAEQAR-------QKELEQRAA--AEKAAKQA 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  348 VEIARQMAERQRQEEELLRQQEvalqeAERQKKererqkeiARQVVERKKQEEvrriekARKKSEMEKKERErqQEIARQ 427
Cdd:TIGR02794 108 EQAAKQAEEKQKQAEEAKAKQA-----AEAKAK--------AEAEAERKAKEE------AAKQAEEEAKAKA--AAEAKK 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  428 HAERQRKeeearrqeearlfaeRQKKERERQEEIARQMEEEEKRQREEAEKEEMRKRKIEEERLRKEEEQRIEAQRKAEE 507
Cdd:TIGR02794 167 KAEEAKK---------------KAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADE 231
                         250
                  ....*....|....*...
gi 597837628  508 ERRIEEQLAAREVENQST 525
Cdd:TIGR02794 232 AELGDIFGLASGSNAEKQ 249
PRK12704 PRK12704
phosphodiesterase; Provisional
289-426 4.82e-09

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 59.79  E-value: 4.82e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 289 QQEIARQEAERQRKEEEMRrqqeyaqqmAEMQRAQKEMEWQREIARQKAEMDEKEKQRQVEIARQMAERQRQEEEL---- 364
Cdd:PRK12704  32 KIKEAEEEAKRILEEAKKE---------AEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLdrkl 102
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 597837628 365 --LRQQEVALQEAERQKKERERQKEIARQVVERKKQEEVRRIEKAR-------KKSEMEKKERERQQEIAR 426
Cdd:PRK12704 103 elLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISgltaeeaKEILLEKVEEEARHEAAV 173
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
270-400 5.36e-09

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


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 55.82  E-value: 5.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  270 EIARQVAERQQKERE--ELEWQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEWQREIARQKAEMDEKEKQRQ 347
Cdd:pfam05672  11 EAARILAEKRRQAREqrEREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRKAEEEAEEREQ 90
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 597837628  348 VEIARQMAERQRQEEELLRQQEvalqEAERQKKERERQKEIARQV-VERKKQEE 400
Cdd:pfam05672  91 REQEEQERLQKQKEEAEAKARE----EAERQRQEREKIMQQEEQErLERKKRIE 140
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
261-426 7.37e-09

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 59.54  E-value: 7.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  261 EQLERQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRR-QQEYAQQMAEMQRAQKEMEWQ--REIARQKA 337
Cdd:COG4913   266 AARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERlEARLDALREELDELEAQIRGNggDRLEQLER 345
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  338 EMDEKEKQRQveiaRQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVERKKQEEVRRIEKARKKSEMEKKE 417
Cdd:COG4913   346 EIERLERELE----ERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRREL 421

                  ....*....
gi 597837628  418 RERQQEIAR 426
Cdd:COG4913   422 RELEAEIAS 430
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
258-432 7.43e-09

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 59.40  E-value: 7.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 258 AEMEQLERQRQqEIARQVAERQQKEREELEWQQEIARQEAERQRKEEE---MRRQQEYAQQMAEMQRAQKEMEwqrEIAR 334
Cdd:COG4717   71 KELKELEEELK-EAEEKEEEYAELQEELEELEEELEELEAELEELREElekLEKLLQLLPLYQELEALEAELA---ELPE 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 335 QKAEMDEKEKqrqvEIARQMAERQRQEEELLR-QQEVALQEAERQKKERERQKEIARQVveRKKQEEVRRIEKARKKSEM 413
Cdd:COG4717  147 RLEELEERLE----ELRELEEELEELEAELAElQEELEELLEQLSLATEEELQDLAEEL--EELQQRLAELEEELEEAQE 220
                        170
                 ....*....|....*....
gi 597837628 414 EKKERERQQEIARQHAERQ 432
Cdd:COG4717  221 ELEELEEELEQLENELEAA 239
PTZ00121 PTZ00121
MAEBL; Provisional
338-519 8.96e-09

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 59.77  E-value: 8.96e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  338 EMDEKEKQRQVEiarqMAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVERKKQEEVRRIEKARKKSEMEKKE 417
Cdd:PTZ00121 1080 DFDAKEDNRADE----ATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVE 1155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  418 RERQQEIARQhaerqrkeeearrqeearlFAERQKKERERQEEIARQmeeeekrQREEAEKEEMRKrkieeerlrkEEE- 496
Cdd:PTZ00121 1156 IARKAEDARK-------------------AEEARKAEDAKKAEAARK-------AEEVRKAEELRK----------AEDa 1199
                         170       180
                  ....*....|....*....|...
gi 597837628  497 QRIEAQRKAEEERRIEEQLAARE 519
Cdd:PTZ00121 1200 RKAEAARKAEEERKAEEARKAED 1222
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
264-521 1.04e-08

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: 59.21  E-value: 1.04e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   264 ERQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEWQREIARQKAEMDEKE 343
Cdd:pfam02463  647 GLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADR 726
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   344 KQRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERER---QKEIARQVVERKKQEEVRRIEKARKKSEMEKKERER 420
Cdd:pfam02463  727 VQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSelsLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRAL 806
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   421 QQE----IARQHAERQRKEEEARRQEEARLFAERQKKERERQEEIARQMEEEEKRQREEAEKEEMRKRKIEEERLRKEEE 496
Cdd:pfam02463  807 EEElkeeAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKD 886
                          250       260
                   ....*....|....*....|....*
gi 597837628   497 QRIEAQRKAEEERRIEEQLAAREVE 521
Cdd:pfam02463  887 ELESKEEKEKEEKKELEEESQKLNL 911
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
252-541 1.04e-08

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: 59.21  E-value: 1.04e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   252 EEGSSNAEMEQLERQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQMA-----EMQRAQKEM 326
Cdd:pfam02463  244 ELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKvddeeKLKESEKEK 323
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   327 EW-QREIARQKAEMDEKEKQRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVERKKQEEVRRIE 405
Cdd:pfam02463  324 KKaEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEE 403
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   406 KARKKSEMEkkERERQQEIARqhAERQRKEEEARRQEEARLFAERQKKERERQEEIARQMEEEEKRQREEAEKEEMRKRK 485
Cdd:pfam02463  404 EKEAQLLLE--LARQLEDLLK--EEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQL 479
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 597837628   486 IEEERLRKEEEQRIEAQRKAEEERRIEEQLAAREVENQSTVVNPAFGMHIPGETQA 541
Cdd:pfam02463  480 VKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLG 535
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
250-523 1.47e-08

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: 58.83  E-value: 1.47e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   250 NFEEGSSNAEMEQLERQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEWQ 329
Cdd:pfam02463  740 LLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEE 819
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   330 REIARQKAEMDEKEKQRQVEIARQMAERQRQ--EEELLRQQEVALQEAERQKKERERQKEiarqvverKKQEEVRRIEKA 407
Cdd:pfam02463  820 EQLLIEQEEKIKEEELEELALELKEEQKLEKlaEEELERLEEEITKEELLQELLLKEEEL--------EEQKLKDELESK 891
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   408 RKKSEMEKKERERQQEIARQHAERQRKEEEARRQEEARLFAERQKKER--------ERQEEIARQMEEEEKRQREEAEKE 479
Cdd:pfam02463  892 EEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEEllleeadeKEKEENNKEEEEERNKRLLLAKEE 971
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 597837628   480 EMRK--RKIEEERLRKEEEQRIEAQRKAEEERRIEEQLAAREVENQ 523
Cdd:pfam02463  972 LGKVnlMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQ 1017
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
202-517 1.53e-08

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: 58.53  E-value: 1.53e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   202 LKQLVRIVEAHQVAINKIEEQVGEERRRggVEDHEHPAGSFRKQGPSGNFEEGSSNAEMEQLERQRQQEIARQvaERQQK 281
Cdd:TIGR02168  679 IEELEEKIEELEEKIAELEKALAELRKE--LEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI--AQLSK 754
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   282 EREELEWQQEIARQEAERQRkEEEMRRQQEYAQQMAEMQRAQKEMEWQREIARQKaemdEKEKQRQVEIARQMAERQRQE 361
Cdd:TIGR02168  755 ELTELEAEIEELEERLEEAE-EELAEAEAEIEELEAQIEQLKEELKALREALDEL----RAELTLLNEEAANLRERLESL 829
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   362 EELLRQQEVALQEAERQKKERERQKEIARQVVErkkqEEVRRIEKARKKSEMEKKERERQQEIARQHAERQRKEEEARRQ 441
Cdd:TIGR02168  830 ERRIAATERRLEDLEEQIEELSEDIESLAAEIE----ELEELIEELESELEALLNERASLEEALALLRSELEELSEELRE 905
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 597837628   442 EEARLFAERQKKERERQEEIARQMEEEEKRQREEAEKEEMRKRKIEEERLRKEEEQRIEAQRKAEEER--RIEEQLAA 517
Cdd:TIGR02168  906 LESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRlkRLENKIKE 983
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
275-532 1.93e-08

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


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 57.74  E-value: 1.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 275 VAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQmAEMQRAQKEMEWQREIARQKAEMDEKEKQRQVEIARQM 354
Cdd:COG3064    1 AQEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEE-ERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 355 AERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVERKKQEEVRRIEKARKKSEMEKKERERQQEIARQHAERQRK 434
Cdd:COG3064   80 AEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 435 EEEARRQEEARLFAERQKKERERQEEIARQMEEEEKRQREEAEKEEMRKRKIEEERLRKEEEQRIEAQRKAEEERRIEEQ 514
Cdd:COG3064  160 AAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEA 239
                        250
                 ....*....|....*...
gi 597837628 515 LAAREVENQSTVVNPAFG 532
Cdd:COG3064  240 TEEAALGGAEEAADLAAV 257
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
257-457 2.12e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 57.86  E-value: 2.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 257 NAEMEQLERQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEWQREIARQK 336
Cdd:COG4717   52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLY 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 337 AEMDEKEkqrqveiaRQMAERQRQEEELLRQQEvALQEAERQKKERERQKEIARQVVERKKQ-------EEVRRIEKARK 409
Cdd:COG4717  132 QELEALE--------AELAELPERLEELEERLE-ELRELEEELEELEAELAELQEELEELLEqlslateEELQDLAEELE 202
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 597837628 410 KSEMEKKERERQQEIARQHAERQRKEEEARRQEEARLFAERQKKERER 457
Cdd:COG4717  203 ELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARL 250
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
259-530 2.40e-08

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: 58.06  E-value: 2.40e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   259 EMEQLERQRQQEIARQVAERQQKEREELEwQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEWQREIARQKAE 338
Cdd:pfam02463  713 KKLKLEAEELLADRVQEAQDKINEELKLL-KQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEE 791
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   339 MDEKEKQRQVEIARQMAERQRQEEELLRqqevaLQEAERQ--KKERERQKEIARQVVERKKQEEvRRIEKARKKSEMEKK 416
Cdd:pfam02463  792 KEEKLKAQEEELRALEEELKEEAELLEE-----EQLLIEQeeKIKEEELEELALELKEEQKLEK-LAEEELERLEEEITK 865
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   417 ERERQQEIARQHAERQRKEEEARRQEEARLFAERQKKERERQEEIARQMEEEEKRQREEAEKEEMRKRKIEEERLRKEEE 496
Cdd:pfam02463  866 EELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEA 945
                          250       260       270
                   ....*....|....*....|....*....|....
gi 597837628   497 QRIEAQRKAEEERRIEEQLAAREVENQSTVVNPA 530
Cdd:pfam02463  946 DEKEKEENNKEEEEERNKRLLLAKEELGKVNLMA 979
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
272-463 2.61e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.02  E-value: 2.61e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 272 ARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEWQREIARQKAEMDEKEKQRQVEIA 351
Cdd:COG1196  579 LDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSA 658
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 352 RQ-MAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVERKKQEEVRRIEKARKKSEMEKKERERQQEIARQHAE 430
Cdd:COG1196  659 GGsLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELL 738
                        170       180       190
                 ....*....|....*....|....*....|...
gi 597837628 431 RQRKEEEARRQEEARLFAERQKKERERQEEIAR 463
Cdd:COG1196  739 EELLEEEELLEEEALEELPEPPDLEELERELER 771
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
252-410 2.77e-08

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


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 56.78  E-value: 2.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  252 EEGSSNAEMEQLERQRQQEIARQVAERQQKEREElewqQEIARQEAERQRKEEEMRRQQEY-AQQMAEMQRAQKemewQR 330
Cdd:TIGR02794  74 EQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQA----EQAAKQAEEKQKQAEEAKAKQAAeAKAKAEAEAERK----AK 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  331 EIARQKAEmDEKEKQRQVEIARQMAERQRQEEELLRQQEVALQ--EAERQKKERERQKEIARQVVERKKQEEVRRIEKAR 408
Cdd:TIGR02794 146 EEAAKQAE-EEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAkaKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAE 224

                  ..
gi 597837628  409 KK 410
Cdd:TIGR02794 225 AE 226
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
327-526 4.64e-08

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 56.35  E-value: 4.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 327 EWQReIARQKAEMDEKEKQRQVEIARQMAE-RQRQEEELLRQQEVAlQEAERQKKERERQKEIARQVVERKKQEE---VR 402
Cdd:PRK09510  63 QYNR-QQQQQKSAKRAEEQRKKKEQQQAEElQQKQAAEQERLKQLE-KERLAAQEQKKQAEEAAKQAALKQKQAEeaaAK 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 403 RIEKARKKSEMEKKereRQQEIARQHAERQRKEEEARRQEEARlfAERQKKERERQEEIARQMEEEEKRQREEAEKEEMR 482
Cdd:PRK09510 141 AAAAAKAKAEAEAK---RAAAAAKKAAAEAKKKAEAEAAKKAA--AEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEA 215
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 597837628 483 KRKIEEERLRKEEEQRIEAQRKAEEERRIEEQLAAREVENQSTV 526
Cdd:PRK09510 216 KKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
DUF4175 pfam13779
Domain of unknown function (DUF4175);
252-427 5.08e-08

Domain of unknown function (DUF4175);


Pssm-ID: 463981 [Multi-domain]  Cd Length: 833  Bit Score: 56.92  E-value: 5.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  252 EEGSSNAEMEQLE---RQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQ--MAEMQRAQKEM 326
Cdd:pfam13779 503 ERGASDEEIAKLMqelREALDDYMQALAEQAQQNPQDLQQPDDPNAQEMTQQDLQRMLDRIEELARSgrRAEAQQMLSQL 582
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  327 ewQREIAR-QKAEMDekekQRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERE--------RQKEIARQVVERKK 397
Cdd:pfam13779 583 --QQMLENlQAGQPQ----QQQQQGQSEMQQAMDELGDLLREQQQLLDETFRQLQQQGgqqqgqpgQQGQQGQGQQPGQG 656
                         170       180       190
                  ....*....|....*....|....*....|
gi 597837628  398 QEEVRRIEKARKKSEMEKKERERQQEIARQ 427
Cdd:pfam13779 657 GQQPGAQMPPQGGAEALGDLAERQQALRRR 686
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
261-420 7.70e-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: 7.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 261 EQLERQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEWQREIARQKAEMD 340
Cdd:COG1196  649 VTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEE 728
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 341 EKEKQRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIAR-------------QVVERKK--QEEVRRIE 405
Cdd:COG1196  729 QLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAlgpvnllaieeyeELEERYDflSEQREDLE 808
                        170       180
                 ....*....|....*....|
gi 597837628 406 KARKK-----SEMEKKERER 420
Cdd:COG1196  809 EARETleeaiEEIDRETRER 828
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
203-392 1.04e-07

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


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 54.85  E-value: 1.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  203 KQLVRIVEAHQVAINKIEEQVGEERRRGGVEDHEHPAGSFRKQGPSGNFEEGSSNAEMEQLERQRQQEIARQVAERQQKE 282
Cdd:TIGR02794  65 KEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKA 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  283 REELEWQQEI---ARQEAERQRKEEEMRRQQEY---AQQMAEMQRAQKEMEWQREIARQKAEMDEKEKQRQVEIARQMAE 356
Cdd:TIGR02794 145 KEEAAKQAEEeakAKAAAEAKKKAEEAKKKAEAeakAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAE 224
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 597837628  357 RQRQEEEL-LRQQEVALQEAERQKKERERQKEIARQV 392
Cdd:TIGR02794 225 AERKADEAeLGDIFGLASGSNAEKQGGARGAAAGSEV 261
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
279-518 1.04e-07

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: 55.83  E-value: 1.04e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   279 QQKEREELEwqQEIARQE---AERQRKEEEMRRQQEYAQQMAEMQRAQKEmewqrEIARQKAEMDEKEKQRQVEIARQMA 355
Cdd:TIGR02168  675 RRREIEELE--EKIEELEekiAELEKALAELRKELEELEEELEQLRKELE-----ELSRQISALRKDLARLEAEVEQLEE 747
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   356 ERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVERKKQEEVRRIEKA---RKKSEMEKKERERQQEIARQHAERQ 432
Cdd:TIGR02168  748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKalrEALDELRAELTLLNEEAANLRERLE 827
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   433 RKEEEARRQEEARLFAERQKKE-RERQEEIARQMEEEEKRQREEAEK-----EEMRKRKIEEERLRKEEEQRIEAQRKAE 506
Cdd:TIGR02168  828 SLERRIAATERRLEDLEEQIEElSEDIESLAAEIEELEELIEELESEleallNERASLEEALALLRSELEELSEELRELE 907
                          250
                   ....*....|..
gi 597837628   507 EERRIEEQLAAR 518
Cdd:TIGR02168  908 SKRSELRRELEE 919
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
252-422 1.76e-07

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 54.43  E-value: 1.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 252 EEGSSNAEMEQlERQRQQEIARQVAERQQKEREELEWQ-QEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKemewQR 330
Cdd:PRK09510  90 EELQQKQAAEQ-ERLKQLEKERLAAQEQKKQAEEAAKQaALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKK----AA 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 331 EIARQKAEMDEKEKQRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVERKKQEEVRRIEKARKK 410
Cdd:PRK09510 165 AEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAA 244
                        170
                 ....*....|..
gi 597837628 411 SEMEKKERERQQ 422
Cdd:PRK09510 245 KAAEKAAAAKAA 256
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
261-559 1.81e-07

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


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 54.66  E-value: 1.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 261 EQLERQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQeyAQQMAEMQRA---QKEMEWQREIARQKA 337
Cdd:COG3064    3 EALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQ--AEEEAREAKAeaeQRAAELAAEAAKKLA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 338 EMDEKEKQRQVEIARQMAERQRQEEELLRQQEvALQEAERQKKERERQKeiARQVVERKKQEEVRRIEKARKKSEMEKKE 417
Cdd:COG3064   81 EAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEK-AAAAAEKEKAEEAKRK--AEEEAKRKAEEERKAAEAEAAAKAEAEAA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 418 RERQQEIARQHAERQRKEEEARRQEEARLFAERQKKERERQEEIARQMEEEEKRQREEAEKEEMRKRKIEEERLRKEEEQ 497
Cdd:COG3064  158 RAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAV 237
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 597837628 498 RIEAQRKAEEERRIEEQLAAREVENQSTVVNPAFGMHIPGETQAGEHSTDYYGYSTNSDATK 559
Cdd:COG3064  238 EATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDD 299
PRK12704 PRK12704
phosphodiesterase; Provisional
269-426 2.21e-07

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 54.40  E-value: 2.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 269 QEIARQVAERQQKEREELEWQQEI-ARQEAERQRKEEEmrrqQEYAQQMAEMQRAQKEMEWQREIARQKAEMDEKEKQrq 347
Cdd:PRK12704  37 EEEAKRILEEAKKEAEAIKKEALLeAKEEIHKLRNEFE----KELRERRNELQKLEKRLLQKEENLDRKLELLEKREE-- 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 348 vEIARQMAERQRQEEELLRQQEVALQEAERQKKERER----QKEIARQVVERKKQEEVRRiEKARKKSEMEKKERERQQE 423
Cdd:PRK12704 111 -ELEKKEKELEQKQQELEKKEEELEELIEEQLQELERisglTAEEAKEILLEKVEEEARH-EAAVLIKEIEEEAKEEADK 188

                 ...
gi 597837628 424 IAR 426
Cdd:PRK12704 189 KAK 191
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
199-402 2.33e-07

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 54.64  E-value: 2.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 199 DEFLKQLVRI-VEAHQVAINKIEEQVGEERRRggVEDHEHPAGSFRKQGPSGNFEEGSS---------NAEMEQLERQRQ 268
Cdd:COG3206  159 EAYLEQNLELrREEARKALEFLEEQLPELRKE--LEEAEAALEEFRQKNGLVDLSEEAKlllqqlselESQLAEARAELA 236
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 269 QEIARQVAERQQKEREELEWQ--------QEIARQEAERQRKEEEMRRQqeYAQQMAEMQRAQKEMEWQREIARQKAEMD 340
Cdd:COG3206  237 EAEARLAALRAQLGSGPDALPellqspviQQLRAQLAELEAELAELSAR--YTPNHPDVIALRAQIAALRAQLQQEAQRI 314
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 597837628 341 EKEKQRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVER--KKQEEVR 402
Cdd:COG3206  315 LASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESllQRLEEAR 378
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
258-388 2.53e-07

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 54.45  E-value: 2.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 258 AEMEQLERQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMrrQQEYAQQMAEmqrAQKemewqrEIARQKA 337
Cdd:PRK00409 523 ASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEA--EKEAQQAIKE---AKK------EADEIIK 591
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 597837628 338 EMDEKEKQRQVEIARQmaerqrQEEELLRQQEVALQEAE-RQKKERERQKEI 388
Cdd:PRK00409 592 ELRQLQKGGYASVKAH------ELIEARKRLNKANEKKEkKKKKQKEKQEEL 637
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
277-519 3.04e-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: 54.19  E-value: 3.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  277 ERQQKEREELEWQQ-EIARQEAERQRKE-EEMRRQQEYAQQMAEMQRAQKEMEWQReiarqKAEMDEKEKQRQVEiarqm 354
Cdd:pfam15709 329 EQEKASRDRLRAERaEMRRLEVERKRREqEEQRRLQQEQLERAEKMREELELEQQR-----RFEEIRLRKQRLEE----- 398
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  355 aERQRQEEELLRQqevALQEAERQKKERERQKEIARQVVERKKQEEVRRIEKArkksemeKKERERQQEIARQHAERQRK 434
Cdd:pfam15709 399 -ERQRQEEEERKQ---RLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERA-------EAEKQRQKELEMQLAEEQKR 467
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  435 EEEARRQeearlfaERQKKERERQEEiarqmeeeekrqreeaekEEMRKRKIEEERLRKEeeqriEAQRKAEEERRIEEQ 514
Cdd:pfam15709 468 LMEMAEE-------ERLEYQRQKQEA------------------EEKARLEAEERRQKEE-----EAARLALEEAMKQAQ 517

                  ....*
gi 597837628  515 LAARE 519
Cdd:pfam15709 518 EQARQ 522
CCDC66 pfam15236
Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil ...
313-432 3.24e-07

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


Pssm-ID: 434558 [Multi-domain]  Cd Length: 154  Bit Score: 50.56  E-value: 3.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  313 AQQMAE-MQRAQKEMEWQREIarqKAEMDEKEKQRQVEIARQMAERQRQEEELLRQqevalQEAERQKKERERQKEIARQ 391
Cdd:pfam15236  41 PAQLEErERKRQKALEHQNAI---KKQLEEKERQKKLEEERRRQEEQEEEERLRRE-----REEEQKQFEEERRKQKEKE 112
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 597837628  392 VVERKKQEEVRR-IEKARKKSEMEKKERERQQEIARQHAERQ 432
Cdd:pfam15236 113 EAMTRKTQALLQaMQKAQELAQRLKQEQRIRELAEKGHDTSQ 154
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
280-424 3.45e-07

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: 52.96  E-value: 3.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 280 QKEREELEwqqEIARQEAERQRKEEE-----MRRQQEYAQQMAEMQRAQKEMEWQREIARQKAEMDEKEKQRqveiarqM 354
Cdd:cd16269  148 LEDREKLV---EKYRQVPRKGVKAEEvlqefLQSKEAEAEAILQADQALTEKEKEIEAERAKAEAAEQERKL-------L 217
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 597837628 355 AERQRQEEELLRQQEVALQEAERQ---KKERERQKEIARQvveRKKQEEVRRIEKARKKSEMEKKERERQQEI 424
Cdd:cd16269  218 EEQQRELEQKLEDQERSYEEHLRQlkeKMEEERENLLKEQ---ERALESKLKEQEALLEEGFKEQAELLQEEI 287
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
258-535 3.60e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 53.37  E-value: 3.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 258 AEMEQLERQRQQeiARQVAERQQKEREELEwqQEIARQEAERQRKEEEMRR--------QQEYAQQMAEMQRAQKEME-W 328
Cdd:COG4372   38 FELDKLQEELEQ--LREELEQAREELEQLE--EELEQARSELEQLEEELEElneqlqaaQAELAQAQEELESLQEEAEeL 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 329 QREIARQKAEMDEKEKQRQV------EIARQMAERQRQEEELLRQQEVALQEAERQKKERERQ-KEIARQVVERKKQEEV 401
Cdd:COG4372  114 QEELEELQKERQDLEQQRKQleaqiaELQSEIAEREEELKELEEQLESLQEELAALEQELQALsEAEAEQALDELLKEAN 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 402 RRIEKARKKSEMEKKERERQQEIARQHAERQRKEEEARRQEEARLF-AERQKKERERQEEIARQMEEEEKRQREEAEKEE 480
Cdd:COG4372  194 RNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLdALELEEDKEELLEEVILKEIEELELAILVEKDT 273
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 597837628 481 MRKRKIEEERLRKEEEQRIEAQRKAEEERRIEEQLAAREVENQSTVVNPAFGMHI 535
Cdd:COG4372  274 EEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKL 328
Nop53 pfam07767
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ...
309-419 3.92e-07

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


Pssm-ID: 462259 [Multi-domain]  Cd Length: 353  Bit Score: 53.07  E-value: 3.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  309 QQEYAQQMAEMQRAQKEMEWQREIARQKAEMDEKEKQRqveiarqMAERQRQEEELLRQQEVALQEAERQKKER---ERQ 385
Cdd:pfam07767 202 QKAVEAEKKRLKEEEKLERVLEKIAESAATAEAREEKR-------KTKAQRNKEKRRKEEEREAKEEKALKKKLaqlERL 274
                          90       100       110
                  ....*....|....*....|....*....|....
gi 597837628  386 KEIARQVVERKKQEEVRRIEKARKKSEMEKKERE 419
Cdd:pfam07767 275 KEIAKEIAEKEKEREEKAEARKREKRKKKKEEKK 308
rne PRK10811
ribonuclease E; Reviewed
264-398 4.19e-07

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 53.89  E-value: 4.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  264 ERQRQQEIARQVAERQQKEREELEWQQEIARQeaeRQRKEEEMRRQQEYAQQMAEMQRaqkemewqreiaRQKAEMDEKE 343
Cdd:PRK10811  601 ERQQDRRKPRQNNRRDRNERRDTRDNRTRREG---RENREENRRNRRQAQQQTAETRE------------SQQAEVTEKA 665
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 597837628  344 KQRQVEIARQMAERQ--RQEEELLRQQEVALQEAERQKKERERQKEIARQVVERKKQ 398
Cdd:PRK10811  666 RTQDEQQQAPRRERQrrRNDEKRQAQQEAKALNVEEQSVQETEQEERVQQVQPRRKQ 722
RNase_Y_N pfam12072
RNase Y N-terminal region;
296-425 4.70e-07

RNase Y N-terminal region;


Pssm-ID: 463456 [Multi-domain]  Cd Length: 201  Bit Score: 51.04  E-value: 4.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  296 EAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEWQREIARQKAEMDEKEKQRQVEIARQmAERQRQEEELLRQQEVALQEA 375
Cdd:pfam12072  26 EAKIGSAEELAKRIIEEAKKEAETKKKEALLEAKEEIHKLRAEAERELKERRNELQRQ-ERRLLQKEETLDRKDESLEKK 104
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 597837628  376 ERQKKERERQKEIARQVVERKKQEEVRRIEKARKKSE--------------MEKKERERQQEIA 425
Cdd:pfam12072 105 EESLEKKEKELEAQQQQLEEKEEELEELIEEQRQELErisgltseeakeilLDEVEEELRHEAA 168
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
264-423 4.96e-07

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: 52.73  E-value: 4.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  264 ERQRQQEIARQVAERQQKEREELEWQQEiarqEAERQRKEEEMRRQQEYAQQMaEMQRAQKEMEWQREIARQKAEMDEKE 343
Cdd:pfam15558  19 EEQRMRELQQQAALAWEELRRRDQKRQE----TLERERRLLLQQSQEQWQAEK-EQRKARLGREERRRADRREKQVIEKE 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  344 KQRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIARqvvERKKQEEVRRIEKA-RKKSEMEKKERERQQ 422
Cdd:pfam15558  94 SRWREQAEDQENQRQEKLERARQEAEQRKQCQEQRLKEKEEELQALR---EQNSLQLQERLEEAcHKRQLKEREEQKKVQ 170

                  .
gi 597837628  423 E 423
Cdd:pfam15558 171 E 171
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
197-513 5.52e-07

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: 53.82  E-value: 5.52e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   197 SEDEFLKQLVRIVEAHQVAINKIEEQVGEERRRGGVEDhehpaGSFRKQGPSGNFEEGSSNAEMEQLERQRQQEiarQVA 276
Cdd:pfam02463  716 KLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEE-----KSRLKKEEKEEEKSELSLKEKELAEEREKTE---KLK 787
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   277 ERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEWQREIARQKAEM-DEKEKQRQVEIARQMA 355
Cdd:pfam02463  788 VEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKlAEEELERLEEEITKEE 867
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   356 ERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVERKKQEEvrrIEKARKKSEMEKKERERQQEIARQHAERQRKE 435
Cdd:pfam02463  868 LLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLL---EEKENEIEERIKEEAEILLKYEEEPEELLLEE 944
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   436 EEARRQEEARLFAERQKKER-ERQEEIARQMEEEEKRQREEAEKEEMR----------KRKIEEERLRKEEEQRIEAQRK 504
Cdd:pfam02463  945 ADEKEKEENNKEEEEERNKRlLLAKEELGKVNLMAIEEFEEKEERYNKdelekerleeEKKKLIRAIIEETCQRLKEFLE 1024

                   ....*....
gi 597837628   505 AEEERRIEE 513
Cdd:pfam02463 1025 LFVSINKGW 1033
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
355-517 5.84e-07

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 52.95  E-value: 5.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 355 AERQRQEEELLRQQEVALQEAER----QKKERERQKEIARqvVERKKQEEVRRIEKARKKSEMEKKERERQQEIARQHAE 430
Cdd:COG2268  188 ALGRRKIAEIIRDARIAEAEAEReteiAIAQANREAEEAE--LEQEREIETARIAEAEAELAKKKAEERREAETARAEAE 265
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 431 RQRKEEearrqeearlfAERQKKERERQEEIARQmeeeekrQREEAEKEEMRKRKIEEERLRKEEEQRIEAQRKAEEER- 509
Cdd:COG2268  266 AAYEIA-----------EANAEREVQRQLEIAER-------EREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAEa 327
                        170
                 ....*....|.
gi 597837628 510 ---RIEEQLAA 517
Cdd:COG2268  328 eaeAIRAKGLA 338
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
261-381 6.09e-07

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: 52.19  E-value: 6.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 261 EQLER--QRQQEIARQV--AERQQKEREELEWQQEIARQEAERQRK-EEEMRRQQEyaQQMAEMQRAQKEMewqreIARQ 335
Cdd:cd16269  170 EVLQEflQSKEAEAEAIlqADQALTEKEKEIEAERAKAEAAEQERKlLEEQQRELE--QKLEDQERSYEEH-----LRQL 242
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 597837628 336 KAEMdEKEKQRQVEIARQMAERQRQEEELLrQQEVALQEAERQKKE 381
Cdd:cd16269  243 KEKM-EEERENLLKEQERALESKLKEQEAL-LEEGFKEQAELLQEE 286
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
266-523 7.58e-07

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: 53.05  E-value: 7.58e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   266 QRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEM----RRQQEYAQQMAEMQRAQKEMEWQR------EIARQ 335
Cdd:TIGR00618  222 QVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLkqlrARIEELRAQEAVLEETQERINRARkaaplaAHIKA 301
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   336 KAEMDEKEKQRQVEIARQMAER---------------------------QRQEEELLRQQEVAL---QEAERQKKERER- 384
Cdd:TIGR00618  302 VTQIEQQAQRIHTELQSKMRSRakllmkraahvkqqssieeqrrllqtlHSQEIHIRDAHEVATsirEISCQQHTLTQHi 381
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   385 -----QKEIARQVVERKKQEEVRRIEKARKKSEMEKKERERQQEIARQHAERQrkeeearrQEEARLFAERQKKERERQE 459
Cdd:TIGR00618  382 htlqqQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQE--------LQQRYAELCAAAITCTAQC 453
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 597837628   460 EIARQMEEEEKRQREEAEKEEMR-KRKIEEERLRKEEEQRIEAQRKAEEERRIEEQLAAREVENQ 523
Cdd:TIGR00618  454 EKLEKIHLQESAQSLKEREQQLQtKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQ 518
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
299-431 7.76e-07

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: 52.35  E-value: 7.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  299 RQRKEEEMRRQQEYAQQMAEMQRAQKEMEWQREIARQKAEMDEKEKQRQVEIARQMAERQRQEEELL--RQQEVALQE-- 374
Cdd:pfam15558  16 RHKEEQRMRELQQQAALAWEELRRRDQKRQETLERERRLLLQQSQEQWQAEKEQRKARLGREERRRAdrREKQVIEKEsr 95
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 597837628  375 ----AERQKKERERQKEIARQVVERKKQEEVRRIekaRKKSEMEKKERERQQEIARQHAER 431
Cdd:pfam15558  96 wreqAEDQENQRQEKLERARQEAEQRKQCQEQRL---KEKEEELQALREQNSLQLQERLEE 153
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
253-530 8.49e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 52.21  E-value: 8.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 253 EGSSNAEMEQLERQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQMA-EMQRAQKEMEWQRE 331
Cdd:COG4372   22 TGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNeQLQAAQAELAQAQE 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 332 ----IARQKAEMDEKEKQRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVERKKQEEVRRIEKA 407
Cdd:COG4372  102 elesLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEA 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 408 RKKSEMEKKERERQQEIARQHAERQRKEEEARRQEEARLFAERQKKERERQEEIARQMEEEEKRQREEAEKEEMRKRKIE 487
Cdd:COG4372  182 EQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIE 261
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 597837628 488 EERLRKEEEQRIEAQRKAEEERRIEEQLAAREVENQSTVVNPA 530
Cdd:COG4372  262 ELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNL 304
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
237-427 8.54e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.00  E-value: 8.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  237 HPAGSFRKQGPSGNFEE---GSSNaemeqleRQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYA 313
Cdd:COG4913   585 GNGTRHEKDDRRRIRSRyvlGFDN-------RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYS 657
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  314 QQMAEMQRAQKEM-EWQREIARQKAEMDE-KEKQRQVEIARQMAERQRQEEELLRQQEVALQEA-ERQKKERERQKEIAR 390
Cdd:COG4913   658 WDEIDVASAEREIaELEAELERLDASSDDlAALEEQLEELEAELEELEEELDELKGEIGRLEKElEQAEEELDELQDRLE 737
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 597837628  391 QVVERKKQEEVRRIEKARKKSEMEKKERERQQEIARQ 427
Cdd:COG4913   738 AAEDLARLELRALLEERFAAALGDAVERELRENLEER 774
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
332-461 1.14e-06

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 52.52  E-value: 1.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 332 IARQKAEM-DEKEKQRQVeIARQMAERQRQEEELlRQQEVALQEAERQKKERERQKEIARQVVERKKQEEVRRIEKARK- 409
Cdd:PRK00409 504 IEEAKKLIgEDKEKLNEL-IASLEELERELEQKA-EEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKe 581
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 597837628 410 -KSEME---KKERERQQEIARQHAERQRKEEEARRQEEARLFAERQKKERERQEEI 461
Cdd:PRK00409 582 aKKEADeiiKELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEEL 637
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
243-430 1.17e-06

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


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 51.93  E-value: 1.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  243 RKQGPSGNFeegsSNAEMEQLERQRQQEIARQVAERQQKEREELEWQQEIARQEAER---QRKEEEMRRQQEYAQQMAEM 319
Cdd:pfam05262 161 KKNILSGNV----SDVDTDSISDKKVVEALREDNEKGVNFRRDMTDLKERESQEDAKraqQLKEELDKKQIDADKAQQKA 236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  320 QRAQKEMEWQREIARQKaemdEKEKQRQVEIARQMAERQRQeeellrqqevalQEAERQKKERER-QKEIARQVVERKKQ 398
Cdd:pfam05262 237 DFAQDNADKQRDEVRQK----QQEAKNLPKPADTSSPKEDK------------QVAENQKREIEKaQIEIKKNDEEALKA 300
                         170       180       190
                  ....*....|....*....|....*....|..
gi 597837628  399 EEVRRIEKARKKSEMEKKERERQQEIARQHAE 430
Cdd:pfam05262 301 KDHKAFDLKQESKASEKEAEDKELEAQKKREP 332
Nup88 pfam10168
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ...
268-430 1.21e-06

Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.


Pssm-ID: 462975 [Multi-domain]  Cd Length: 713  Bit Score: 52.35  E-value: 1.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  268 QQEIARQVAERQQKEREELEWQQEIARQEAERQRKeeeMRRQQEyAQQMAEMQRAQKEMEWQREIARQKAEMDEKEKQRQ 347
Cdd:pfam10168 530 PQECLQLLSRATQVFREEYLKKHDLAREEIQKRVK---LLKLQK-EQQLQELQSLEEERKSLSERAEKLAEKYEEIKDKQ 605
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  348 VEIARQMAERQRqeeeLLRQQEVALQEAERQ-KKERERQKEIARQVVER-----KKQEEVRR-IEK---ARKKSEMEKKE 417
Cdd:pfam10168 606 EKLMRRCKKVLQ----RLNSQLPVLSDAEREmKKELETINEQLKHLANAikqakKKMNYQRYqIAKsqsIRKKSSLSLSE 681
                         170
                  ....*....|....*
gi 597837628  418 RERQ--QEIARQHAE 430
Cdd:pfam10168 682 KQRKtiKEILKQLGS 696
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
254-463 1.50e-06

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: 52.38  E-value: 1.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   254 GSSNAEMEQLERQrqqeIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQ-EYAQQMAEMQRAQKEMEWQR-- 330
Cdd:TIGR02169  297 GELEAEIASLERS----IAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERkRRDKLTEEYAELKEELEDLRae 372
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   331 --EIARQKAEMDEKEKQRQVEIarqmAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVERKKQEEVRRIEKAr 408
Cdd:TIGR02169  373 leEVDKEFAETRDELKDYREKL----EKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKA- 447
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 597837628   409 kkSEMEKKERERQQEIARQHAERQRKEEEARRqeearlFAERQKKERERQEEIAR 463
Cdd:TIGR02169  448 --LEIKKQEWKLEQLAADLSKYEQELYDLKEE------YDRVEKELSKLQRELAE 494
CCDC34 pfam13904
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ...
280-410 1.61e-06

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: 50.09  E-value: 1.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  280 QKEREELE-WQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEM---EWQREIARQKAEMDEKEKQRQVEIARQMA 355
Cdd:pfam13904  48 KLERQPLEaYENWLAAKQRQRQKELQAQKEEREKEEQEAELRKRLAKEkyqEWLQRKARQQTKKREESHKQKAAESASKS 127
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 597837628  356 ERQRQEEELLRQQEVALQEAERQKKERE-RQKEIARQVVERKKQEEVRRIEKARKK 410
Cdd:pfam13904 128 LAKPERKVSQEEAKEVLQEWERKKLEQQqRKREEEQREQLKKEEEEQERKQLAEKA 183
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
262-463 1.65e-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: 1.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 262 QLERQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEWQREIARQKAEMDE 341
Cdd:COG1196  578 PLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGS 657
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 342 KEKQRQVEIARQMAERQRQEEELLRQQEVALQEAER-QKKERERQKEIARQVVERKKQEEVRRIEKARKKsemEKKERER 420
Cdd:COG1196  658 AGGSLTGGSRRELLAALLEAEAELEELAERLAEEELeLEEALLAEEEEERELAEAEEERLEEELEEEALE---EQLEAER 734
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 597837628 421 QQEIARQHAERQRKEEEARRQEEARLFAERQKKERER-QEEIAR 463
Cdd:COG1196  735 EELLEELLEEEELLEEEALEELPEPPDLEELERELERlEREIEA 778
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
258-427 1.90e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.84  E-value: 1.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  258 AEMEQLERQRQQEIARQVAERQQKEREELEWQQEIARQE---AERQRKEEEMRRQQEYAQQMAEMQRAQKEMEWQREIAR 334
Cdd:COG4913   286 AQRRLELLEAELEELRAELARLEAELERLEARLDALREEldeLEAQIRGNGGDRLEQLEREIERLERELEERERRRARLE 365
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  335 QKAEM-------DEKEKQRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEiarqvverkkqEEVRRIEka 407
Cdd:COG4913   366 ALLAAlglplpaSAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELE-----------AEIASLE-- 432
                         170       180
                  ....*....|....*....|
gi 597837628  408 RKKSEMEKKERERQQEIARQ 427
Cdd:COG4913   433 RRKSNIPARLLALRDALAEA 452
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
259-523 1.97e-06

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: 51.99  E-value: 1.97e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   259 EMEQLERQRQ-----QEIARQVAERQQKE--REELEWQQEIARQEAERQRKEEEMRRQQEYAQQMA-EMQRAQKEMEwqr 330
Cdd:TIGR02169  199 QLERLRREREkaeryQALLKEKREYEGYEllKEKEALERQKEAIERQLASLEEELEKLTEEISELEkRLEEIEQLLE--- 275
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   331 EIARQKAEMDEKEkqrQVEIARQMAERQRQEEELLRQQEVALQE----AERQKKERERQKEIARQVVERKKQEEVRRIEK 406
Cdd:TIGR02169  276 ELNKKIKDLGEEE---QLRVKEKIGELEAEIASLERSIAEKEREledaEERLAKLEAEIDKLLAEIEELEREIEEERKRR 352
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   407 ARKKSEMEKKERERQ------QEIARQHAERQrkeeearrqeearlfaERQKKERERQEEIARQMeeeEKRQREEAEKEE 480
Cdd:TIGR02169  353 DKLTEEYAELKEELEdlraelEEVDKEFAETR----------------DELKDYREKLEKLKREI---NELKRELDRLQE 413
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 597837628   481 MRKRKIEEERLRKEEEQRIEAQRKAEEERRIEEQLAAREVENQ 523
Cdd:TIGR02169  414 ELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWK 456
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
295-464 2.11e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 51.31  E-value: 2.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 295 QEAERQRKEEEmRRQQEYAQQMAEMQRAQKEME-WQREIARQKAEMDEKEKQRQveiARQMAERQRQEEELLRQQEVALQ 373
Cdd:COG4717   74 KELEEELKEAE-EKEEEYAELQEELEELEEELEeLEAELEELREELEKLEKLLQ---LLPLYQELEALEAELAELPERLE 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 374 EAERQKKE-RERQKEIARQVVERKKQEEVRRIEKARKKSEMEKKERERQQEIARQHAERQRKEEEARRQEEARLFAERQK 452
Cdd:COG4717  150 ELEERLEElRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
                        170
                 ....*....|..
gi 597837628 453 KERERQEEIARQ 464
Cdd:COG4717  230 EQLENELEAAAL 241
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
259-383 2.27e-06

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: 50.69  E-value: 2.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  259 EMEQLERQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEyAQQMAEMQRAQKEMEWQREIARQkae 338
Cdd:pfam13868 223 EREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEE-IEQEEAEKRRMKRLEHRRELEKQ--- 298
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 597837628  339 mdEKEKQRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERE 383
Cdd:pfam13868 299 --IEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKKLKE 341
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
265-527 3.64e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 50.29  E-value: 3.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 265 RQRQQEIARQVAERQQKEREELE-WQQEIARQEAERQRKEEEMRRQQEyaqqmaEMQRAQKEMEWQREIARQKAEMDEKE 343
Cdd:COG4372   19 RPKTGILIAALSEQLRKALFELDkLQEELEQLREELEQAREELEQLEE------ELEQARSELEQLEEELEELNEQLQAA 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 344 KQRQVEIARQMAERQRQEEELlrqqevaLQEAERQKKERERQKEIARQVVERKKQEEVRRIEKARKKSEMEKKERERQQE 423
Cdd:COG4372   93 QAELAQAQEELESLQEEAEEL-------QEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 424 IARQHAERQRKEEEARRQEEARLFAE-RQKKERERQEEIARQMEEEEKRQREEAEKEEMRKRKIEEERLRKEEEQRIEAQ 502
Cdd:COG4372  166 LAALEQELQALSEAEAEQALDELLKEaNRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE 245
                        250       260
                 ....*....|....*....|....*
gi 597837628 503 RKAEEERRIEEQLAAREVENQSTVV 527
Cdd:COG4372  246 EDKEELLEEVILKEIEELELAILVE 270
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
196-484 3.95e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 50.84  E-value: 3.95e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   196 MSEDefLKQLVRIVEAHQVAINKIEEQVGEERRRggVEDHEHPAGSFRKQGPSGNFEEGSSNAEMEQLERQRQQ------ 269
Cdd:TIGR02169  679 LRER--LEGLKRELSSLQSELRRIENRLDELSQE--LSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSleqeie 754
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   270 ----EIARQVAERQQKEREELEWQQEIARQEAER-----QRKEEEMRRQQEYAQ----QMAEMQRAQKEMEWQREIARQK 336
Cdd:TIGR02169  755 nvksELKELEARIEELEEDLHKLEEALNDLEARLshsriPEIQAELSKLEEEVSrieaRLREIEQKLNRLTLEKEYLEKE 834
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   337 AEmdeKEKQRQVEIARQMAERQRQEEEL-LRQQEVALQEAERQKKERE---RQKEIARQVVERKKQEEVRRIEKARKKSE 412
Cdd:TIGR02169  835 IQ---ELQEQRIDLKEQIKSIEKEIENLnGKKEELEEELEELEAALRDlesRLGDLKKERDELEAQLRELERKIEELEAQ 911
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   413 MEKKE-RERQQEIARQHAE----------RQRKEEEARRQEEARLFAERQKKERERQ--------------EEIARQMEE 467
Cdd:TIGR02169  912 IEKKRkRLSELKAKLEALEeelseiedpkGEDEEIPEEELSLEDVQAELQRVEEEIRalepvnmlaiqeyeEVLKRLDEL 991
                          330
                   ....*....|....*..
gi 597837628   468 EEKRQREEAEKEEMRKR 484
Cdd:TIGR02169  992 KEKRAKLEEERKAILER 1008
PKK pfam12474
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino ...
274-405 4.15e-06

Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino acids in length. The family is found in association with pfam00069. Polo-like kinase 1 (Plx1) is essential during mitosis for the activation of Cdc25C, for spindle assembly, and for cyclin B degradation. This family is Polo kinase kinase (PKK) which phosphorylates Polo kinase and Polo-like kinase to activate them. PKK is a serine/threonine kinase.


Pssm-ID: 463600 [Multi-domain]  Cd Length: 139  Bit Score: 47.17  E-value: 4.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  274 QVAERQQKEREELEWQQEIARQEAERqrkeEEMRRQQEyaQQMAEMQRAQkEMEWQREIARQKAEMDEKEKQRQVEIARQ 353
Cdd:pfam12474   2 QLQKEQQKDRFEQERQQLKKRYEKEL----EQLERQQK--QQIEKLEQRQ-TQELRRLPKRIRAEQKKRLKMFRESLKQE 74
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 597837628  354 MAERqRQEEELLRQQEvaLQEAERQKKERERQKEIARQVVERKKQEEVRRIE 405
Cdd:pfam12474  75 KKEL-KQEVEKLPKFQ--RKEAKRQRKEELELEQKHEELEFLQAQSEALERE 123
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
258-512 4.45e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 50.84  E-value: 4.45e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   258 AEMEQLERQRQQ---EIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRR--QQEYAQQMAEMQRAQKEMEW---- 328
Cdd:TIGR02169  230 KEKEALERQKEAierQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDlgEEEQLRVKEKIGELEAEIASlers 309
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   329 QREIARQKAEMDEKEKQRQVEIARQMAERQRQEEELLRQQ--EVALQEAERQKKERERQKEIARQVVERKKQEEVRRIEK 406
Cdd:TIGR02169  310 IAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERkrRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD 389
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   407 ARKKSEMEKKERE-------RQQEIARQHAERQRKEEEARRQEEARL--FAERQKKERERQEEIARQMEEEEKRQREEAE 477
Cdd:TIGR02169  390 YREKLEKLKREINelkreldRLQEELQRLSEELADLNAAIAGIEAKIneLEEEKEDKALEIKKQEWKLEQLAADLSKYEQ 469
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 597837628   478 KEEMRKRKIEE----ERLRKEEEQRIEAQRKAEEERRIE 512
Cdd:TIGR02169  470 ELYDLKEEYDRvekeLSKLQRELAEAEAQARASEERVRG 508
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
314-409 5.27e-06

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: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 46.80  E-value: 5.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  314 QQMAEMQRAQKEME-----WQREIARQKAEMDEKEKQRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEI 388
Cdd:pfam03938  12 EESPEGKAAQAQLEkkfkkRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLQQKAQQELQKKQQE 91
                          90       100
                  ....*....|....*....|.
gi 597837628  389 ARQVVERKKQEEVRRIEKARK 409
Cdd:pfam03938  92 LLQPIQDKINKAIKEVAKEKG 112
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
255-432 5.32e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 49.83  E-value: 5.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 255 SSNAEMEQLERQRQQeiARQVAERQQKEREELewQQEIARQEAERQRKEEEMrrqqeyAQQMAEMQRAQKEMEW------ 328
Cdd:COG3883   41 ALQAELEELNEEYNE--LQAELEALQAEIDKL--QAEIAEAEAEIEERREEL------GERARALYRSGGSVSYldvllg 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 329 --------------QREIARQKAEMDE-KEKQRQVEIARQMAERQRQE-EELLRQQEVALQEAERQKKERERQ-KEIARQ 391
Cdd:COG3883  111 sesfsdfldrlsalSKIADADADLLEElKADKAELEAKKAELEAKLAElEALKAELEAAKAELEAQQAEQEALlAQLSAE 190
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 597837628 392 VVERKKQEEVRRIEKARKKSEMEKKERERQQEIARQHAERQ 432
Cdd:COG3883  191 EAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
255-464 5.52e-06

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: 49.76  E-value: 5.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 255 SSNAEMEQLERQR---QQEIARQVAERQQKEREELEWQQEIARQEAERQRKEeemRRQQEYAQQMAEMQRAQKEMewQRE 331
Cdd:COG4942   17 AQADAAAEAEAELeqlQQEIAELEKELAALKKEEKALLKQLAALERRIAALA---RRIRALEQELAALEAELAEL--EKE 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 332 IARQKAEMDEKEKQ-RQVEIARQMAERQRQEEELLRQQEVAlqeaerqkkERERQKEIARQVVERKKQeevrRIEKARKK 410
Cdd:COG4942   92 IAELRAELEAQKEElAELLRALYRLGRQPPLALLLSPEDFL---------DAVRRLQYLKYLAPARRE----QAEELRAD 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 597837628 411 SEmEKKERERQQEIARQHAERQRKEEEARRQEEARLFAERQKKERERQEEIARQ 464
Cdd:COG4942  159 LA-ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAEL 211
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
318-423 6.11e-06

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 50.21  E-value: 6.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 318 EMQRAQKEMEWQR-EIARQKAEmdeKEKQrqvEIARQMAERQRQEEELLRQQEVALQEAERQKKE---------RERQKE 387
Cdd:PRK00409 526 EELERELEQKAEEaEALLKEAE---KLKE---ELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKeadeiikelRQLQKG 599
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 597837628 388 IARQVVERKKQEEVRRIEKARKKSEMEKKERERQQE 423
Cdd:PRK00409 600 GYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQE 635
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
288-521 6.24e-06

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: 49.38  E-value: 6.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 288 WQQEIARQEAERQRKEeemrRQQEYAQQMAEMQRAQKEmewQREIARQKAEMDEKEKQRQVEIARQMAERQRQEEELlrq 367
Cdd:COG4942   16 AAQADAAAEAEAELEQ----LQQEIAELEKELAALKKE---EKALLKQLAALERRIAALARRIRALEQELAALEAEL--- 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 368 QEVALQEAERQKKERERQKEIARQVVERKKQEEVRRI----------EKARKKSEMEKKERERQQEIARQHAERQRKEEE 437
Cdd:COG4942   86 AELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLalllspedflDAVRRLQYLKYLAPARREQAEELRADLAELAAL 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 438 ARRqeearLFAERQKKERERQEEIARQmeeeekrQREEAEKEEmrKRKIEEERLRKEEEQRIEAQRKAEEERRIEEQLAA 517
Cdd:COG4942  166 RAE-----LEAERAELEALLAELEEER-------AALEALKAE--RQKLLARLEKELAELAAELAELQQEAEELEALIAR 231

                 ....
gi 597837628 518 REVE 521
Cdd:COG4942  232 LEAE 235
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
259-416 6.85e-06

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 50.05  E-value: 6.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  259 EMEQLERQRQQEIARQVAERQQKEREELEWQQEIARQE--AERQRK-EEEMRRQQEYAQQMAEMQRA-QKEMEWQREIAR 334
Cdd:PRK10929  193 ELAQLSANNRQELARLRSELAKKRSQQLDAYLQALRNQlnSQRQREaERALESTELLAEQSGDLPKSiVAQFKINRELSQ 272
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  335 ----QKAEMDE-KEKQRQveiARQMAERQRQEEELLRQQ------EVALQEAERQKKER--ERQK------EIARQVVER 395
Cdd:PRK10929  273 alnqQAQRMDLiASQQRQ---AASQTLQVRQALNTLREQsqwlgvSNALGEALRAQVARlpEMPKpqqldtEMAQLRVQR 349
                         170       180
                  ....*....|....*....|.
gi 597837628  396 KKQEEVrrIEKARKKSEMEKK 416
Cdd:PRK10929  350 LRYEDL--LNKQPQLRQIRQA 368
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
208-432 7.09e-06

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 50.05  E-value: 7.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  208 IVEAHQVAINKIEEQVGEERR----RGGVEDHEHPAGSFRKQGPSGNFEEGSSNAEM--EQLERQRQQ------EIARQV 275
Cdd:PRK10929   46 IVEALQSALNWLEERKGSLERakqyQQVIDNFPKLSAELRQQLNNERDEPRSVPPNMstDALEQEILQvssqllEKSRQA 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  276 AERQQKERE------ELEWQQEiarqEAERQRKEEEMRRQQEYAQQ--MAEMQRAQKemewQREIARQKAEMDEKE---- 343
Cdd:PRK10929  126 QQEQDRAREisdslsQLPQQQT----EARRQLNEIERRLQTLGTPNtpLAQAQLTAL----QAESAALKALVDELElaql 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  344 --KQRQvEIARQMAE-RQRQEEEL-LRQQEVALQEAERQKKERERQKEIARQVVERKKQ---EEVRRIEKARKKSEMEKK 416
Cdd:PRK10929  198 saNNRQ-ELARLRSElAKKRSQQLdAYLQALRNQLNSQRQREAERALESTELLAEQSGDlpkSIVAQFKINRELSQALNQ 276
                         250
                  ....*....|....*.
gi 597837628  417 ERERQQEIARQhaERQ 432
Cdd:PRK10929  277 QAQRMDLIASQ--QRQ 290
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
258-464 7.69e-06

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: 49.26  E-value: 7.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  258 AEMEQLERQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMR-RQQEYA-QQMAEMQRAQKEMEWQR----- 330
Cdd:pfam15558  72 ARLGREERRRADRREKQVIEKESRWREQAEDQENQRQEKLERARQEAEQRkQCQEQRlKEKEEELQALREQNSLQlqerl 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  331 EIARQKAEMDEKEKQRQV------EIARQMA-----ERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVER--KK 397
Cdd:pfam15558 152 EEACHKRQLKEREEQKKVqennlsELLNHQArkvlvDCQAKAEELLRRLSLEQSLQRSQENYEQLVEERHRELREKaqKE 231
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 597837628  398 QEEVRRIEKARKKSEMEKKER--------ERQQEIARQHAERQRKEEEARrqeearlfAERQKKERERQEEIARQ 464
Cdd:pfam15558 232 EEQFQRAKWRAEEKEEERQEHkealaelaDRKIQQARQVAHKTVQDKAQR--------ARELNLEREKNHHILKL 298
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
265-462 7.88e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 49.06  E-value: 7.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 265 RQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEyaqqmaEMQRAQKE-MEWQREIARQKAEMDE-- 341
Cdd:COG3883   19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQA------EIDKLQAEiAEAEAEIEERREELGEra 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 342 KEKQRQ----------------------VEIARQMAERQRqeeELLRQQEVALQEAERQKKERERQKEIARQVV----ER 395
Cdd:COG3883   93 RALYRSggsvsyldvllgsesfsdfldrLSALSKIADADA---DLLEELKADKAELEAKKAELEAKLAELEALKaeleAA 169
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 597837628 396 KKQEEVRRIEKARKKSEMEKKERERQQEIARQHAERQRKEEEARRQEEARLFAERQKKERERQEEIA 462
Cdd:COG3883  170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
258-426 7.94e-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: 7.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 258 AEMEQLERQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEM-----RRQQEYAQQMAEMQRAQKEMEWQREI 332
Cdd:COG1196  605 ASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGeggsaGGSLTGGSRRELLAALLEAEAELEEL 684
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 333 ARQKAEMDEKEKQRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVERKKQEEVRRIEKARKKSE 412
Cdd:COG1196  685 AERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEE 764
                        170
                 ....*....|....
gi 597837628 413 MEKKERERQQEIAR 426
Cdd:COG1196  765 LERELERLEREIEA 778
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
343-464 7.98e-06

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


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 46.57  E-value: 7.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  343 EKQRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVERKKQEEVRRIEKARKKSEMEKKERERQQ 422
Cdd:pfam05672  18 EKRRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRKAEEEAEEREQREQEEQE 97
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 597837628  423 EIARQHAERQRKEEEArrqeearlfAERQKKERER---QEEIARQ 464
Cdd:pfam05672  98 RLQKQKEEAEAKAREE---------AERQRQEREKimqQEEQERL 133
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
314-424 8.21e-06

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: 47.14  E-value: 8.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 314 QQMAEMQRAQKEMEwqreiarqkaemdEKEKQRQVEIARQMAERQRQEEELLRQQEVaLQEAERQKKERErqkeIarqvv 393
Cdd:COG2825   36 QESPEGKAAQKKLE-------------KEFKKRQAELQKLEKELQALQEKLQKEAAT-LSEEERQKKERE----L----- 92
                         90       100       110
                 ....*....|....*....|....*....|.
gi 597837628 394 eRKKQEEVRRIEKARKKsEMEKKERERQQEI 424
Cdd:COG2825   93 -QKKQQELQRKQQEAQQ-DLQKRQQELLQPI 121
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
258-564 8.50e-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: 8.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 258 AEMEQLERQRQQEIARQVAERQQKEREE--LEWQQEIARQEAERQRKEEEMRRQQEyAQQMAEMQRAQKEMEWQREIARQ 335
Cdd:COG3064   39 AEEERLAELEAKRQAEEEAREAKAEAEQraAELAAEAAKKLAEAEKAAAEAEKKAA-AEKAKAAKEAEAAAAAEKAAAAA 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 336 KAEMDEKEKQRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVERKKQEEVRRIEKARKKSEMEK 415
Cdd:COG3064  118 EKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAA 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 416 KERERQQEIARQHAERQRKEEEARRQEEARLFAERQKKERERQEEIARQMEEEEKRQREEAEKEEMRKRKIEEERLRKEE 495
Cdd:COG3064  198 AAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSG 277
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 597837628 496 EQRIEAQRKAEEERRIEEQLAAREVENQSTVVNPAFGMHIPGETQAGEHSTDYYGYSTNSDATKTVLAG 564
Cdd:COG3064  278 LVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAA 346
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
304-464 8.68e-06

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: 8.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  304 EEMRRQQEYAQQMAEMQRAQKEMEWQREIARQkaemdEKEKQRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERE 383
Cdd:COG4913   245 EDAREQIELLEPIRELAERYAAARERLAELEY-----LRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLD 319
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  384 RQKEIARQVVERKKQEEVRRIEKARKKSEMEKKERERQQEiARQHAERQRKEEEARRQEEARLFAERQKKERERQEEIAR 463
Cdd:COG4913   320 ALREELDELEAQIRGNGGDRLEQLEREIERLERELEERER-RRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEE 398

                  .
gi 597837628  464 Q 464
Cdd:COG4913   399 E 399
vATP-synt_E pfam01991
ATP synthase (E/31 kDa) subunit; This family includes the vacuolar ATP synthase E subunit, as ...
259-416 9.47e-06

ATP synthase (E/31 kDa) subunit; This family includes the vacuolar ATP synthase E subunit, as well as the archaebacterial ATP synthase E subunit.


Pssm-ID: 396537 [Multi-domain]  Cd Length: 199  Bit Score: 47.37  E-value: 9.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  259 EMEQLERQRQQEIARQVAERQQKEREELEWQQEIA-RQEAERQRKEEEMRRQQEYAQQMAEMQRaqKEMEWQREIARqka 337
Cdd:pfam01991   1 FIRQEAEEKAEEIRAKAEEEFAIEKAELVQEAEEKiDEIYEKKEKQAEMQKKIIISNAKNEARL--KVLEAREEILD--- 75
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 597837628  338 EMDEKEKQRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVERKKQEevrrIEKARKKSEMEKK 416
Cdd:pfam01991  76 EVFNEAEKKLAELEEDTDEYKDLLRKLIVQALVKLGEPEVIVRCRKRDEELVESALDKAAEE----YKAKTKKVTVEKA 150
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
257-410 1.14e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.14  E-value: 1.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  257 NAEMEQLERQRQQEIARQVAERQQKER--EELEW---QQEIARQEAERQRKE------EEMRRQQEYAQqmAEMQRAQKE 325
Cdd:COG4913   630 EERLEALEAELDALQERREALQRLAEYswDEIDVasaEREIAELEAELERLDassddlAALEEQLEELE--AELEELEEE 707
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  326 mewQREIARQKAEMDEKEKQRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVERKKQEEvRRIE 405
Cdd:COG4913   708 ---LDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALR-ARLN 783

                  ....*
gi 597837628  406 KARKK 410
Cdd:COG4913   784 RAEEE 788
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
266-357 1.16e-05

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: 45.51  E-value: 1.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 266 QRQQEIARQV--AERQQKEREEL--EWQQEI--ARQEAERQRKEEEMRRQQEYAQQMAEMQR-AQKEME-WQREIARQKA 337
Cdd:cd06503   30 EREEKIAESLeeAEKAKEEAEELlaEYEEKLaeARAEAQEIIEEARKEAEKIKEEILAEAKEeAERILEqAKAEIEQEKE 109
                         90       100
                 ....*....|....*....|
gi 597837628 338 EMDEKEKQRQVEIARQMAER 357
Cdd:cd06503  110 KALAELRKEVADLAVEAAEK 129
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
290-432 1.39e-05

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: 47.23  E-value: 1.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 290 QEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEmEWQREIARQKAEMDEKEKQRQVEIARQMAER-QRQEEELlrQQ 368
Cdd:COG1579   20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELE-DLEKEIKRLELEIEEVEARIKKYEEQLGNVRnNKEYEAL--QK 96
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 597837628 369 EVALQEAERQKKErERQKEIARQVVERKKQEEVRRIEKARKKSEMEKKERERQQEIARQHAERQ 432
Cdd:COG1579   97 EIESLKRRISDLE-DEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELE 159
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
261-369 1.58e-05

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


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 44.91  E-value: 1.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  261 EQLERQRQQEIAR--QVAERQQKEREELEWQQEIARQ-EAERQRKEEEMRRQQEYAQQMAEMQR-----AQKEMEWQREI 332
Cdd:pfam20492   2 EEAEREKQELEERlkQYEEETKKAQEELEESEETAEElEEERRQAEEEAERLEQKRQEAEEEKErleesAEMEAEEKEQL 81
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 597837628  333 ARQKAEMDEKEKQRQVEIARQMAERQRQEEELLRQQE 369
Cdd:pfam20492  82 EAELAEAQEEIARLEEEVERKEEEARRLQEELEEARE 118
PRK12705 PRK12705
hypothetical protein; Provisional
265-430 1.62e-05

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 48.55  E-value: 1.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 265 RQRQQEIARQVAERQQKEREELEWQQEIARQE---AERQRKEEEMRRQQEyaqqmaEMQRAQKEMEWQREIARQKAEMDE 341
Cdd:PRK12705  28 RQRLAKEAERILQEAQKEAEEKLEAALLEAKElllRERNQQRQEARRERE------ELQREEERLVQKEEQLDARAEKLD 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 342 KEKQRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKErERQKEIARQVVERKKQEEVRRIEKARKKSEMEKKERERQ 421
Cdd:PRK12705 102 NLENQLEEREKALSARELELEELEKQLDNELYRVAGLTPE-QARKLLLKLLDAELEEEKAQRVKKIEEEADLEAERKAQN 180
                        170
                 ....*....|..
gi 597837628 422 ---QEIARQHAE 430
Cdd:PRK12705 181 ilaQAMQRIASE 192
CCDC50_N pfam15295
Coiled-coil domain-containing protein 50 N-terminus;
329-403 1.63e-05

Coiled-coil domain-containing protein 50 N-terminus;


Pssm-ID: 464621 [Multi-domain]  Cd Length: 126  Bit Score: 45.10  E-value: 1.63e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 597837628  329 QREIARQKAEMDEKEKQRQVEIARQMAERQRQEEELLRQ-QEVALQEAERQKKERERQKEIARQVVERKKQEEVRR 403
Cdd:pfam15295  50 QNDIRVAKQLQEEEELQAQTLFQRRLAQLEEQDEEIAKEiQEELQREAEERRRREEEDEEIARQLQERERERERRR 125
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
261-367 1.68e-05

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 48.79  E-value: 1.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  261 EQLERQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEeemrrqqeyaQQMAEMQRAQKEMEWQREIARQKAEMD 340
Cdd:PRK11448  141 ENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALE----------GLAAELEEKQQELEAQLEQLQEKAAET 210
                          90       100
                  ....*....|....*....|....*...
gi 597837628  341 EKE-KQRQVEIARQMAERQRQEEELLRQ 367
Cdd:PRK11448  211 SQErKQKRKEITDQAAKRLELSEEETRI 238
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
276-394 1.74e-05

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: 45.12  E-value: 1.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 276 AERQQKEREELEwQQEIARQEAERQrkeeemrrQQEYAQQMAEmqrAQKEMEWQREIARQKAemdEKEKQRQVEIARQMA 355
Cdd:cd06503   29 DEREEKIAESLE-EAEKAKEEAEEL--------LAEYEEKLAE---ARAEAQEIIEEARKEA---EKIKEEILAEAKEEA 93
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 597837628 356 ERQRQEEellrQQEValqEAERQKKERERQKEIARQVVE 394
Cdd:cd06503   94 ERILEQA----KAEI---EQEKEKALAELRKEVADLAVE 125
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
266-463 2.09e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.23  E-value: 2.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 266 QRQQEIARQVAERQQKEREELEWQQEIAR----QEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEWQREIARQKAEMDE 341
Cdd:COG4717  299 SLGKEAEELQALPALEELEEEELEELLAAlglpPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAE 378
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 342 KeKQRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERErqkEIARQVVERKKQEEVRRIEKARKksEMEKKERERQ 421
Cdd:COG4717  379 A-GVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELE---ELLEALDEEELEEELEELEEELE--ELEEELEELR 452
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 597837628 422 QEIARQHAERQRKEEEARRQEEARLFAERQKKERERQEEIAR 463
Cdd:COG4717  453 EELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAA 494
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
259-411 2.36e-05

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


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 48.08  E-value: 2.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  259 EMEQLERQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQE------------------YAQQMAEMQ 320
Cdd:pfam05262 205 ERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAknlpkpadtsspkedkqvAENQKREIE 284
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  321 RAQKEmewqreiARQKAEMDEKEKQRQVEIARQMAERQRQEEEllrqqevalQEAERQKKERERQKEIARQVVERKKQEE 400
Cdd:pfam05262 285 KAQIE-------IKKNDEEALKAKDHKAFDLKQESKASEKEAE---------DKELEAQKKREPVAEDLQKTKPQVEAQP 348
                         170
                  ....*....|.
gi 597837628  401 VRRIEKARKKS 411
Cdd:pfam05262 349 TSLNEDAIDSS 359
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
252-518 2.40e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.39  E-value: 2.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 252 EEGSSNAEMEQLERQRQQEIARQVAERQQKErEELEWQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEWQRE 331
Cdd:COG1196  503 YEGFLEGVKAALLLAGLRGLAGAVAVLIGVE-AAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDK 581
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 332 IARQKAEMDEKEKQRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVERKKQEEVRRIEKARKKS 411
Cdd:COG1196  582 IRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGS 661
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 412 EMEKKERERQQEIARQHAERQRKEEEARRQEEARLFAERQKKERERQEEIARQMEEEEKRQREEAEKEEMRKRKIEEERL 491
Cdd:COG1196  662 LTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEEL 741
                        250       260
                 ....*....|....*....|....*..
gi 597837628 492 RKEEEQRIEAQRKAEEERRIEEQLAAR 518
Cdd:COG1196  742 LEEEELLEEEALEELPEPPDLEELERE 768
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
298-524 2.52e-05

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 48.04  E-value: 2.52e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   298 ERQRKEEEMRRQQEYaqqMAEMQRAQKEME----------WQREIARQKAEMDEKEKQRQVEIARQMAERQRQEEEL--- 364
Cdd:pfam02463  154 RRLEIEEEAAGSRLK---RKKKEALKKLIEetenlaeliiDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLyld 230
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   365 ---LRQQEVALQEAERQKKERERQKEIARQVVERKKQEEVRRI--EKARKKSEMEKK-----ERERQQEIARQHAERQRK 434
Cdd:pfam02463  231 ylkLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKEnkEEEKEKKLQEEElkllaKEEEELKSELLKLERRKV 310
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   435 EEEARRQEEARLFAERQKKERERQEEIARQMEEEEKRQREEAEKEEMRK------RKIEEERLRKEEEQRIEAQRKAEEE 508
Cdd:pfam02463  311 DDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEeleklqEKLEQLEEELLAKKKLESERLSSAA 390
                          250
                   ....*....|....*.
gi 597837628   509 RRIEEQLAAREVENQS 524
Cdd:pfam02463  391 KLKEEELELKSEEEKE 406
Caldesmon pfam02029
Caldesmon;
220-521 2.57e-05

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 47.94  E-value: 2.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  220 EEQVGEERRRGGVEDhehpagsFRKQGPSGnfEEGSSNAEMEQLERQRQQEIARQVAERQQKEREE----LEWQQEiaRQ 295
Cdd:pfam02029   4 EEEAARERRRRAREE-------RRRQKEEE--EPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEeeafLDRTAK--RE 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  296 EAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEwqREIARQKAEMDEKEKQRQVEIARQMAE----RQRQEEELLRQQEVA 371
Cdd:pfam02029  73 ERRQKRLQEALERQKEFDPTIADEKESVAERK--ENNEEEENSSWEKEEKRDSRLGRYKEEeteiREKEYQENKWSTEVR 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  372 lQEAERQKKERERQKEIARQVVERKKQEEVR--RIEKARKKSEMEKKERERQQEIARQHAE------------------- 430
Cdd:pfam02029 151 -QAEEEGEEEEDKSEEAEEVPTENFAKEEVKdeKIKKEKKVKYESKVFLDQKRGHPEVKSQngeeevtklkvttkrrqgg 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  431 ---RQRKEEEARRQEEARLFAERQKK---ERERQE-EIARQMEEEEKRQREEAEKEEMRKRKIEEERLRKEEEQRIEAQR 503
Cdd:pfam02029 230 lsqSQEREEEAEVFLEAEQKLEELRRrrqEKESEEfEKLRQKQQEAELELEELKKKREERRKLLEEEEQRRKQEEAERKL 309
                         330
                  ....*....|....*....
gi 597837628  504 KAEEE-RRIEEQLAAREVE 521
Cdd:pfam02029 310 REEEEkRRMKEEIERRRAE 328
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
266-357 2.59e-05

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: 45.16  E-value: 2.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 266 QRQQEIARQV--AERQQKEREEL--EWQQEI--ARQEAERQRKE--EEMRRQQEYAQQMAEMQRAQKEMEWQREIARQKA 337
Cdd:COG0711   31 ERQEKIADGLaeAERAKEEAEAAlaEYEEKLaeARAEAAEIIAEarKEAEAIAEEAKAEAEAEAERIIAQAEAEIEQERA 110
                         90       100
                 ....*....|....*....|
gi 597837628 338 EMDEKEKQRQVEIARQMAER 357
Cdd:COG0711  111 KALAELRAEVADLAVAIAEK 130
fliH PRK06669
flagellar assembly protein H; Validated
252-389 2.61e-05

flagellar assembly protein H; Validated


Pssm-ID: 235850 [Multi-domain]  Cd Length: 281  Bit Score: 46.93  E-value: 2.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 252 EEGSSNAEMEQLERQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQMAE-----MQRAQKEM 326
Cdd:PRK06669  56 EAKEIIEEAEEDAFEIVEAAEEEAKEELLKKTDEASSIIEKLQMQIEREQEEWEEELERLIEEAKAEgyeegYEKGREEG 135
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 597837628 327 EwqreiarqkAEMDEKEKQRQVEIARQMAERQRQ----EEELLrqqEVALQEAERQKKER-ERQKEIA 389
Cdd:PRK06669 136 L---------EEVRELIEQLNKIIEKLIKKREEIlessEEEIV---ELALDIAKKVIKEIsENSKEIA 191
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
251-431 2.68e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.84  E-value: 2.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 251 FEEGSSNAEMEQLERQRQQEIARQVAERQQKEREEL--------EWQQ---EIARQEAERQRKEEEMRRQQEYAQQMAEM 319
Cdd:COG4717  304 AEELQALPALEELEEEELEELLAALGLPPDLSPEELlelldrieELQEllrEAEELEEELQLEELEQEIAALLAEAGVED 383
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 320 --------QRAQKEMEWQREIARQKAEMDEKEKQRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQ 391
Cdd:COG4717  384 eeelraalEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELE 463
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 597837628 392 VVERKKQEEVRRIEKARKKSEMEKKERERQ-QEIARQHAER 431
Cdd:COG4717  464 QLEEDGELAELLQELEELKAELRELAEEWAaLKLALELLEE 504
PTZ00491 PTZ00491
major vault protein; Provisional
266-432 2.77e-05

major vault protein; Provisional


Pssm-ID: 240439 [Multi-domain]  Cd Length: 850  Bit Score: 48.09  E-value: 2.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 266 QRQQEIARQVAERQ-QKEREELEWQQEIARQEAERQRKEeemrrqqeYAQQMAEMQRAQKEMEwQREIARQKAEMDEKEK 344
Cdd:PTZ00491 662 KSQEAAARHQAELLeQEARGRLERQKMHDKAKAEEQRTK--------LLELQAESAAVESSGQ-SRAEALAEAEARLIEA 732
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 345 QRQVEIARQMAERQRQEEEllrqqevALQEAERQKKERERQKEIARQVVERKKQEEVRRIEKARKKSEMEKKERERQQEI 424
Cdd:PTZ00491 733 EAEVEQAELRAKALRIEAE-------AELEKLRKRQELELEYEQAQNELEIAKAKELADIEATKFERIVEALGRETLIAI 805

                 ....*...
gi 597837628 425 ARQHAERQ 432
Cdd:PTZ00491 806 ARAGPELQ 813
RIB43A pfam05914
RIB43A; This family consists of several RIB43A-like eukaryotic proteins. Ciliary and flagellar ...
258-365 3.10e-05

RIB43A; This family consists of several RIB43A-like eukaryotic proteins. Ciliary and flagellar microtubules contain a specialized set of protofilaments, termed ribbons, that are composed of tubulin and several associated proteins. RIB43A was first characterized in the unicellular biflagellate, Chlamydomonas reinhardtii although highly related sequences are present in several higher eukaryotes including humans. The function of this protein is unknown although the structure of RIB43A and its association with the specialized protofilament ribbons and with basal bodies is relevant to the proposed role of ribbons in forming and stabilising doublet and triplet microtubules and in organizing their three-dimensional structure. Human RIB43A homologs could represent a structural requirement in centriole replication in dividing cells.


Pssm-ID: 461780 [Multi-domain]  Cd Length: 372  Bit Score: 47.20  E-value: 3.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  258 AEMEQLERQRQQ-----EI-----------ARQVAERQ---------------QKEREELEWQQEIARQEAERQRkEEEM 306
Cdd:pfam05914 219 AERRRLEKRQEQednlaEIynhltsdllteNPEVAQSSlgphrvipdrwkgmsPEQLKEIRKEQEQQREEKERRR-EEEK 297
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 597837628  307 RRQQEYAQQMAEMQRAQkeMEWQREIARQKAEMdekeKQRQVEIARQMAERQRQEEELL 365
Cdd:pfam05914 298 QRDAEWDRQRLELARAA--LLLEREQQRLRREL----RRQLDEENLQLAQEQKARQEYL 350
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
259-401 3.24e-05

Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.


Pssm-ID: 284517 [Multi-domain]  Cd Length: 749  Bit Score: 47.82  E-value: 3.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  259 EMEQLERQRQQEIARQVAERQQKEREELE---WQQEIARQEAERQRKE-----EEMRRQQEYAQQMAEMQRAQKEMEWQR 330
Cdd:pfam07111 513 EQGEAERQQLSEVAQQLEQELQRAQESLAsvgQQLEVARQGQQESTEEaaslrQELTQQQEIYGQALQEKVAEVETRLRE 592
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 597837628  331 EIARQKAEMDE--KEKQRQVEIARQMAERQRQEEEllRQQEVALQEAERQKKERERqkeIARQVVERKKQEEV 401
Cdd:pfam07111 593 QLSDTKRRLNEarREQAKAVVSLRQIQHRATQEKE--RNQELRRLQDEARKEEGQR---LARRVQELERDKNL 660
growth_prot_Scy NF041483
polarized growth protein Scy;
264-547 4.06e-05

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 47.51  E-value: 4.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  264 ERQRQQEIARQVAERQQKErEELEWqqeiARQEAERQRKE-----EEMRRQQEYA----QQMAEMQRAQKEMEWQREIAR 334
Cdd:NF041483  505 ERVRTEAIERATTLRRQAE-ETLER----TRAEAERLRAEaeeqaEEVRAAAERAarelREETERAIAARQAEAAEELTR 579
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  335 QKAEMDEK--EKQRQVEIARQMAERQRQE--EELLRQQEVA------LQEAERQKKERERQKEIARQVVERKKQEEVRRI 404
Cdd:NF041483  580 LHTEAEERltAAEEALADARAEAERIRREaaEETERLRTEAaerirtLQAQAEQEAERLRTEAAADASAARAEGENVAVR 659
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  405 EKARKKSEMEKKERERQQEIARQHAERQRKEEEARRQEEARLFAERQKKERERqeeiaRQMEEEEKRQREEAEKEEMRKR 484
Cdd:NF041483  660 LRSEAAAEAERLKSEAQESADRVRAEAAAAAERVGTEAAEALAAAQEEAARRR-----REAEETLGSARAEADQERERAR 734
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 597837628  485 KIEEERLRKEEEQRIEAQRKA-----EEERRIEEQLAAREVENQStVVNPAFGMH------IPGETQAGEHSTD 547
Cdd:NF041483  735 EQSEELLASARKRVEEAQAEAqrlveEADRRATELVSAAEQTAQQ-VRDSVAGLQeqaeeeIAGLRSAAEHAAE 807
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
258-405 4.14e-05

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 47.64  E-value: 4.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  258 AEMEQLERQRQ----------QEIARQVAERQQKEREELEwqqeiarQEAERQRKEEEMRRQQEyaqQMAEMQRAQKEME 327
Cdd:COG3096   522 AELEQRLRQQQnaerlleefcQRIGQQLDAAEELEELLAE-------LEAQLEELEEQAAEAVE---QRSELRQQLEQLR 591
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  328 WQREIARQKAEMDEKekqrqveiARQMAERQRQE--EELLRQQEValQEAERQKKERERQKEIARQVVERKKQEEVRRIE 405
Cdd:COG3096   592 ARIKELAARAPAWLA--------AQDALERLREQsgEALADSQEV--TAAMQQLLEREREATVERDELAARKQALESQIE 661
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
247-522 4.32e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 47.37  E-value: 4.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   247 PSGNFEEGSSNAEMEQLERQRQQEIARQVAERQQK-EREELEWQQEIARQEAERQRKEEEMRR-QQEYAQQMAEMQRAQK 324
Cdd:TIGR02169  651 KSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGlKRELSSLQSELRRIENRLDELSQELSDaSRKIGEIEKEIEQLEQ 730
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   325 EMEWQREIARQKAEmDEKEKQRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIarqvveRKKQEEVRRI 404
Cdd:TIGR02169  731 EEEKLKERLEELEE-DLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRI------PEIQAELSKL 803
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   405 EKARkkSEMEKKERERQQEIARQHAERQrkeeearrqeearlFAERQKKERERQeeiarqmeeeekrqREE-AEKEEMRK 483
Cdd:TIGR02169  804 EEEV--SRIEARLREIEQKLNRLTLEKE--------------YLEKEIQELQEQ--------------RIDlKEQIKSIE 853
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 597837628   484 RKIEEERLRKEEEQRiEAQRKAEEERRIEEQLA--AREVEN 522
Cdd:TIGR02169  854 KEIENLNGKKEELEE-ELEELEAALRDLESRLGdlKKERDE 893
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
271-416 4.40e-05

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 47.16  E-value: 4.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 271 IARQVAERQQKEREELEwqQEIARQEAERQRKEEEMRRQQEyaqqmaEMQRAQKE-MEWQREIARQKAEMDEKEKqrqvE 349
Cdd:COG2433  382 LEELIEKELPEEEPEAE--REKEHEERELTEEEEEIRRLEE------QVERLEAEvEELEAELEEKDERIERLER----E 449
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 597837628 350 IARqmaERQRQEEELLRQQEValqeaerqkkeRERQKEIARqvVERKKQEEVRRIEKARKKSEMEKK 416
Cdd:COG2433  450 LSE---ARSEERREIRKDREI-----------SRLDREIER--LERELEEERERIEELKRKLERLKE 500
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
294-523 4.42e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.24  E-value: 4.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 294 RQEAERQRK--EEEMRR----QQEYAQQMAEMQRaqkemewQREIARQKAEMDEKEKQRQVEIARQMAERQRQEEELLRQ 367
Cdd:COG1196  174 KEEAERKLEatEENLERlediLGELERQLEPLER-------QAEKAERYRELKEELKELEAELLLLKLRELEAELEELEA 246
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 368 QEVALQEAERQKKERERQKEIARQVVERKKQEEVRRIEKARKKsemekkERERQQEIARQHAERQRKeeearrqeearlf 447
Cdd:COG1196  247 ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAE------EYELLAELARLEQDIARL------------- 307
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 597837628 448 AERQKKERERQEEIARQmeeeekrqreeaekeemrkrkieEERLRkEEEQRIEAQRKAEEERRIEEQLAAREVENQ 523
Cdd:COG1196  308 EERRRELEERLEELEEE-----------------------LAELE-EELEELEEELEELEEELEEAEEELEEAEAE 359
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
273-455 4.68e-05

Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.


Pssm-ID: 284517 [Multi-domain]  Cd Length: 749  Bit Score: 47.05  E-value: 4.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  273 RQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQ--EYAQQM-AEMQRAQKEM-----------EWQREIARQKAE 338
Cdd:pfam07111 484 EQLREERNRLDAELQLSAHLIQQEVGRAREQGEAERQQlsEVAQQLeQELQRAQESLasvgqqlevarQGQQESTEEAAS 563
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  339 MDEKEKQRQVEIARQMAERQRQEEELLRQQevaLQEAERQKKERERQKEIA----RQVvERKKQEEVRRIEKARKKSEME 414
Cdd:pfam07111 564 LRQELTQQQEIYGQALQEKVAEVETRLREQ---LSDTKRRLNEARREQAKAvvslRQI-QHRATQEKERNQELRRLQDEA 639
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 597837628  415 KKerERQQEIARQHAERQRKEEEARRQEEARLFAERQKKER 455
Cdd:pfam07111 640 RK--EEGQRLARRVQELERDKNLMLATLQQEGLLSRYKQQR 678
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
291-521 4.91e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 47.37  E-value: 4.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 291 EIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEWQREIARQKAEMDEKEKQRQVEIARQMAERQRQEEEL---LRQ 367
Cdd:PRK03918 177 RIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLegsKRK 256
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 368 QEVALQEAERQKKE-RERQKEIARQVVE----RKKQEEVRRIEKARKKSEMEKKERERQQEIARQHAERqrkeeearrqe 442
Cdd:PRK03918 257 LEEKIRELEERIEElKKEIEELEEKVKElkelKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEING----------- 325
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 597837628 443 earlfAERQKKERERQEEIARQMeeeekrqreEAEKEEMRKRKIEEERLRKEEEqriEAQRKAEEERRIEEQLAAREVE 521
Cdd:PRK03918 326 -----IEERIKELEEKEERLEEL---------KKKLKELEKRLEELEERHELYE---EAKAKKEELERLKKRLTGLTPE 387
Rabaptin pfam03528
Rabaptin;
265-423 5.46e-05

Rabaptin;


Pssm-ID: 367545 [Multi-domain]  Cd Length: 486  Bit Score: 46.64  E-value: 5.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  265 RQRQQEIARQVAE-RQQKEREELEWQQEIARQEAERQRKEEEMRRQQ--------EYAQQMAEMQRAQKEMEWQREIA-- 333
Cdd:pfam03528   7 QQRVAELEKENAEfYRLKQQLEAEFNQKRAKFKELYLAKEEDLKRQNavlqeaqvELDALQNQLALARAEMENIKAVAtv 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  334 ----RQKAeMDEKEKQRQVEIArqmaERQRQEEELLRQQEValQEAERQKKERERQKEIaRQVVERKKQEEVRRIEKARK 409
Cdd:pfam03528  87 sentKQEA-IDEVKSQWQEEVA----SLQAIMKETVREYEV--QFHRRLEQERAQWNQY-RESAEREIADLRRRLSEGQE 158
                         170
                  ....*....|....
gi 597837628  410 KSEMEKKERERQQE 423
Cdd:pfam03528 159 EENLEDEMKKAQED 172
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
314-407 5.50e-05

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: 43.73  E-value: 5.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   314 QQMAEMQRAQKEMEwqREIARQKAEMDEKEKQrqveiARQMAERQRQEEELLRQQEVALQEAERQKKERE--RQKEIARQ 391
Cdd:smart00935  11 QESPAGKAAQKQLE--KEFKKRQAELEKLEKE-----LQKLKEKLQKDAATLSEAAREKKEKELQKKVQEfqRKQQKLQQ 83
                           90
                   ....*....|....*.
gi 597837628   392 VVERKKQEEVRRIEKA 407
Cdd:smart00935  84 DLQKRQQEELQKILDK 99
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
258-379 8.21e-05

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 46.61  E-value: 8.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 258 AEMEQLERQRQQ-EIARQVAERQQKE--REELEwqqEIARQEAERQRKEEEMRRQQEyaqqmAEMQRAQKEMEWQREIAR 334
Cdd:COG0542  411 EELDELERRLEQlEIEKEALKKEQDEasFERLA---ELRDELAELEEELEALKARWE-----AEKELIEEIQELKEELEQ 482
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 597837628 335 QKAEMDEKEKQRQvEIARQMAERQRQEEELLRQQEVA-------------LQEAERQK 379
Cdd:COG0542  483 RYGKIPELEKELA-ELEEELAELAPLLREEVTEEDIAevvsrwtgipvgkLLEGEREK 539
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
293-397 8.59e-05

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: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 43.33  E-value: 8.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  293 ARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEwqreiaRQKAEMDEKEKQRQVEIARQMAERQRQEEEllRQQEVAL 372
Cdd:pfam03938  16 EGKAAQAQLEKKFKKRQAELEAKQKELQKLYEELQ------KDGALLEEEREEKEQELQKKEQELQQLQQK--AQQELQK 87
                          90       100
                  ....*....|....*....|....*
gi 597837628  373 QEAERQKKERERQKEIARQVVERKK 397
Cdd:pfam03938  88 KQQELLQPIQDKINKAIKEVAKEKG 112
PRK05035 PRK05035
electron transport complex protein RnfC; Provisional
265-486 8.86e-05

electron transport complex protein RnfC; Provisional


Pssm-ID: 235334 [Multi-domain]  Cd Length: 695  Bit Score: 46.09  E-value: 8.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 265 RQRQQEIARQVAERQQKEReelewqqeiARQ--EAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEWQREIARQKAEMDEK 342
Cdd:PRK05035 432 RQAKAEIRAIEQEKKKAEE---------AKArfEARQARLEREKAAREARHKKAAEARAAKDKDAVAAALARVKAKKAAA 502
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 343 EKQRQVEIARQ------MAERQ-RQEEELLRQQEVALQEAERQKKErERQKEIARqvVERKKQEevRRIEKARKKSEMEK 415
Cdd:PRK05035 503 TQPIVIKAGARpdnsavIAAREaRKAQARARQAEKQAAAAADPKKA-AVAAAIAR--AKAKKAA--QQAANAEAEEEVDP 577
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 597837628 416 KERERQQEIARQHAERQRKEEEARRQEEARLFAERQKKERERQEEIARQMEEEEKRQREEAEKEEMRKRKI 486
Cdd:PRK05035 578 KKAAVAAAIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAV 648
GAF COG2203
GAF domain [Signal transduction mechanisms];
269-527 9.74e-05

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 46.34  E-value: 9.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 269 QEIARQVA---ERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEWQREIARQKAEMDEKEKQ 345
Cdd:COG2203  334 EALADQAAiaiERARLYEALEAALAALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDAADLS 413
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 346 RQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVERKKQEEVRRIEKARKKSEMEKKERERQQEIA 425
Cdd:COG2203  414 GLLALEGLLLLDLLLLLLLLRRILLLRVLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVILLALALLAALLLLLLL 493
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 426 RQHAERQRKEEEARRQEEARLFAERQKKERERQEEIARQMEEEEKRQREEAEKEEMRKRKIEEERLRKEEEQRIEAQRKA 505
Cdd:COG2203  494 LLALLALSALAVLASLLLALLLLLLLLLLLLLLGLLAALAADLLLLAAALLEDLLILLLVLLLERELLTLVGVLLLLGLS 573
                        250       260
                 ....*....|....*....|..
gi 597837628 506 EEERRIEEQLAAREVENQSTVV 527
Cdd:COG2203  574 VLLIELALALILALALLELLLV 595
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
310-523 1.12e-04

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 45.29  E-value: 1.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  310 QEYAQQMAEMQRAQKEMEWQREIArQKAEMDEKEKQRQVEIARQM-AERQRQEEELLRQQEVALQEAERQKKERERQKEI 388
Cdd:pfam13868   6 DELRELNSKLLAAKCNKERDAQIA-EKKRIKAEEKEEERRLDEMMeEERERALEEEEEKEEERKEERKRYRQELEEQIEE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  389 ARQvvERKKQEEVRRIEKARKKSEMEKKERERQQEIARQHAERQRKEEEARRQEEARLFAERQKKERERQEEIARQMEEE 468
Cdd:pfam13868  85 REQ--KRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLK 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 597837628  469 EKRQREEAEKEEMRKRKIEEERLRKEEEQRIEAQRKAEEERriEEQLAAREVENQ 523
Cdd:pfam13868 163 EKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAER--DELRAKLYQEEQ 215
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
292-411 1.31e-04

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 45.88  E-value: 1.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  292 IARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKemewqreiaRQKAEMDEKEKQRQVEIARQMAERQRQEEELLrqqeva 371
Cdd:PTZ00266  430 VDKDHAERARIEKENAHRKALEMKILEKKRIER---------LEREERERLERERMERIERERLERERLERERL------ 494
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 597837628  372 lqeaERQKKERERQKEIARQVVERKKQEevrRIEKARKKS 411
Cdd:PTZ00266  495 ----ERDRLERDRLDRLERERVDRLERD---RLEKARRNS 527
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
340-518 1.53e-04

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


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 44.84  E-value: 1.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  340 DEKEKQRQV-EIARQMA-ERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVverKKQEEVRRIEKARKKSEMEKKE 417
Cdd:TIGR02794  44 DPGAVAQQAnRIQQQKKpAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRA---AAEKAAKQAEQAAKQAEEKQKQ 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  418 ----RERQQEIARQHAE---RQRKEEEARRQEEARLFAERQKKERERQEEIARQMEEEEKRQREEAEK--EEMRKRKIEE 488
Cdd:TIGR02794 121 aeeaKAKQAAEAKAKAEaeaERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKakAEEAKAKAEA 200
                         170       180       190
                  ....*....|....*....|....*....|
gi 597837628  489 ERLRKEEeqriEAQRKAEEERRIEEQLAAR 518
Cdd:TIGR02794 201 AKAKAAA----EAAAKAEAEAAAAAAAEAE 226
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
257-334 1.54e-04

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: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 42.56  E-value: 1.54e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 597837628  257 NAEMEQLERQRQQEIARQVAERQQKEREeleWQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEWQREIAR 334
Cdd:pfam03938  21 QAQLEKKFKKRQAELEAKQKELQKLYEE---LQKDGALLEEEREEKEQELQKKEQELQQLQQKAQQELQKKQQELLQP 95
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
355-431 1.67e-04

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 45.50  E-value: 1.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  355 AERQRQEEELLRQQ--EVALQEAER-QKKERERQKEIARQVVERKKQEEVRRIEKARKKSEMEKKERERQQEIARQHAER 431
Cdd:PTZ00266  435 AERARIEKENAHRKalEMKILEKKRiERLEREERERLERERMERIERERLERERLERERLERDRLERDRLDRLERERVDR 514
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
343-535 1.73e-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: 44.99  E-value: 1.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  343 EKQRQVEIARQMAE-RQRQEEELLRQQEVALQEAERQKKERERQK----------EIARQVVERKKQEEVRRIEKARKKS 411
Cdd:pfam05262 189 DNEKGVNFRRDMTDlKERESQEDAKRAQQLKEELDKKQIDADKAQqkadfaqdnaDKQRDEVRQKQQEAKNLPKPADTSS 268
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  412 EMEKKERERQQEIARQHAERQRKEEEARRQEEARLFAERQKKERERQEEIARQMEEEEKRQREEAEkEEMRKRKieeerl 491
Cdd:pfam05262 269 PKEDKQVAENQKREIEKAQIEIKKNDEEALKAKDHKAFDLKQESKASEKEAEDKELEAQKKREPVA-EDLQKTK------ 341
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 597837628  492 rkeeeQRIEAQRKAEEERRIEEqlaarevenqstvVNPAFGMHI 535
Cdd:pfam05262 342 -----PQVEAQPTSLNEDAIDS-------------SNPVYGLKV 367
flagell_FliJ TIGR02473
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ...
278-395 1.74e-04

flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly every case, in the midst of other flagellar biosynthesis genes in bacgterial genomes. Typically the fliJ gene is found adjacent to the gene for the flagellum-specific ATPase FliI. Sequence scoring in the gray zone between trusted and noise cutoffs include both probable FliJ proteins and components of bacterial type III secretion systems.


Pssm-ID: 131526 [Multi-domain]  Cd Length: 141  Bit Score: 42.69  E-value: 1.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  278 RQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEWQREIARQKAEMDEK---------EKQRQV 348
Cdd:TIGR02473  12 EKEEEQAKLELAKAQAEFERLETQLQQLIKYREEYEQQALEKVGAGTSALELSNYQRFIRQLDQRiqqqqqelaLLQQEV 91
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 597837628  349 EIARQMAERQRQEE---ELLRQQEVALQEAERQKKERERQKEIARQVVER 395
Cdd:TIGR02473  92 EAKRERLLEARRELkalEKLKEKKQKEYRAEEAKREQKEMDELATQRFRR 141
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
344-425 1.77e-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: 42.42  E-value: 1.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 344 KQRQVEIARQM--AERQRQE-EELLRQQEVALQEAERQKKE-----RERQKEIARQVVERKKQEEVRRIEKARKKSEMEK 415
Cdd:cd06503   29 DEREEKIAESLeeAEKAKEEaEELLAEYEEKLAEARAEAQEiieeaRKEAEKIKEEILAEAKEEAERILEQAKAEIEQEK 108
                         90
                 ....*....|..
gi 597837628 416 KE--RERQQEIA 425
Cdd:cd06503  109 EKalAELRKEVA 120
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
334-523 1.83e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.14  E-value: 1.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 334 RQKAEMDEKEKQRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVErKKQEEVRRIEKARKKSEM 413
Cdd:COG4717   52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELE-ELREELEKLEKLLQLLPL 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 414 EKKERERQQEIAR-----QHAERQRKEEEARRQEEARLFAERQKKERERQEEIARQMEEEEKRQREEAEKEEMRKRKIEE 488
Cdd:COG4717  131 YQELEALEAELAElperlEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAE 210
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 597837628 489 ERLRKEEEQRiEAQRKAEEERRIEEQLAAREVENQ 523
Cdd:COG4717  211 LEEELEEAQE-ELEELEEELEQLENELEAAALEER 244
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
241-425 1.84e-04

Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.


Pssm-ID: 461708 [Multi-domain]  Cd Length: 600  Bit Score: 45.02  E-value: 1.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  241 SFRKQGPSG-NFEEGSSNAEMEQLERQRQQEIARQVAERQQKEREELEWQQEiARQEAERQRKEEEMRRQQEYAQQMAEM 319
Cdd:pfam05667 283 SFSGSSTTDtGLTKGSRFTHTEKLQFTNEAPAATSSPPTKVETEEELQQQRE-EELEELQEQLEDLESSIQELEKEIKKL 361
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  320 QRAQKEMEwqREIARQKAEMDEKEKqrQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIAR----QVVER 395
Cdd:pfam05667 362 ESSIKQVE--EELEELKEQNEELEK--QYKVKKKTLDLLPDAEENIAKLQALVDASAQRLVELAGQWEKHRvpliEEYRA 437
                         170       180       190
                  ....*....|....*....|....*....|
gi 597837628  396 KKQEEVRRIEKARKKSEMEKKERERQQEIA 425
Cdd:pfam05667 438 LKEAKSNKEDESQRKLEEIKELREKIKEVA 467
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
274-481 1.87e-04

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


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 45.20  E-value: 1.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  274 QVAERQQKEREELEWQQeiaRQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEWQREIARQKAEM---DEKEKQRQVEI 350
Cdd:pfam10174 450 RIIERLKEQREREDRER---LEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGlkkDSKLKSLEIAV 526
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  351 ARQMAERQRQEEELLRQQEVALQE---AERQKKERERQKEIARQVVE-RKKQEEVRRIEKARKKSEMEKKERERQQEIAR 426
Cdd:pfam10174 527 EQKKEECSKLENQLKKAHNAEEAVrtnPEINDRIRLLEQEVARYKEEsGKAQAEVERLLGILREVENEKNDKDKKIAELE 606
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 597837628  427 QHAERQRKEEEARRQEEARLFAERQKKERERQEEIARQMEEEEKRQREEAEKEEM 481
Cdd:pfam10174 607 SLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELM 661
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
255-486 2.07e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.05  E-value: 2.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 255 SSNAEMEQLERQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEE------EMRRQQEYAQQ-MAEMQRAQKEME 327
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEElkeeieELEKELESLEGsKRKLEEKIRELE 265
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 328 WQREIARQKAEmDEKEKQRQVEIARQMAERQRQEEELLRQQEVALQEAE-RQKKERERQKEIARQVVER-KKQEEVRRIE 405
Cdd:PRK03918 266 ERIEELKKEIE-ELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEkRLSRLEEEINGIEERIKELeEKEERLEELK 344
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 406 KARKKSE---MEKKERERQQEIARQHAERQRKEEEARRQEEARLFAERQKKERERQEEIARQMEEEEKRQREEAEKEEMR 482
Cdd:PRK03918 345 KKLKELEkrlEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKEL 424

                 ....
gi 597837628 483 KRKI 486
Cdd:PRK03918 425 KKAI 428
PLN02316 PLN02316
synthase/transferase
336-395 2.23e-04

synthase/transferase


Pssm-ID: 215180 [Multi-domain]  Cd Length: 1036  Bit Score: 45.25  E-value: 2.23e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 597837628  336 KAEMDE--------KEKQRQVE-IARQMAERQRQ-EEELLRQQEVALQEAERQ--KKERERQKEIARQVVER 395
Cdd:PLN02316  238 EGGMDEhsfedfllEEKRRELEkLAKEEAERERQaEEQRRREEEKAAMEADRAqaKAEVEKRREKLQNLLKK 309
Agg_substance NF033875
LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, ...
96-341 2.29e-04

LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, are LPXTG-anchored large surface proteins that contribute to virulence. Several closely related paralogs may be found in a single strain.


Pssm-ID: 411439 [Multi-domain]  Cd Length: 1306  Bit Score: 45.09  E-value: 2.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   96 PEPTTVRPYRPVFTTPNrKIVSSAATKSPKPPPTRTTATTLTTPPLKNRKVTEPIPVSEAQMTGMQPSTRGYTRGPQMHT 175
Cdd:NF033875   50 PGTTTVQPDNPDPQSGS-ETPKTAVSEEATVQKDTTSQPTKVEEVASEKNGAEQSSATPNDTTNAQQPTVGAEKSAQEQP 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  176 tgVTAGTTSGEHMVNYKGITMSEDEFLKQLVRIVEAHQVAINKieeQVGEERRRGGVEDHEHPAGSFrkqGPSGNFEEGS 255
Cdd:NF033875  129 --VVSPETTNEPLGQPTEVAPAENEANKSTSIPKEFETPDVDK---AVDEAKKDPNITVVEKPAEDL---GNVSSKDLAA 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  256 SNAEMEQLERQRQQEIARQVAERQQKEREELEWQQEI-ARQEAERQRKEEEMRRQQEYAQQMAEMQRA-QKEMEWQREIA 333
Cdd:NF033875  201 KEKEVDQLQKEQAKKIAQQAAELKAKNEKIAKENAEIaAKNKAEKERYEKEVAEYNKHKNENGYVNEAiSKNLVFDQSVV 280

                  ....*...
gi 597837628  334 RQKAEMDE 341
Cdd:NF033875  281 TKDTKISS 288
MAT1 pfam06391
CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for ...
257-370 2.31e-04

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


Pssm-ID: 461894 [Multi-domain]  Cd Length: 202  Bit Score: 43.38  E-value: 2.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  257 NAEMEQLERQRQQEIARQvAERQQKEREELEWQQEIARQEAERQRKEEemrrqqeyaQQMAEMQRAQKEMEwQREI--AR 334
Cdd:pfam06391  67 EKKIEQYEKENKDLILKN-KMKLSQEEEELEELLELEKREKEERRKEE---------KQEEEEEKEKKEKA-KQELidEL 135
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 597837628  335 QKAEMDEKE--KQRQVEIARQMAERQRQEEELLRQQEV 370
Cdd:pfam06391 136 MTSNKDAEEiiAQHKKTAKKRKSERRRKLEELNRVLEQ 173
ChtBD2 smart00494
Chitin-binding domain type 2;
657-696 2.65e-04

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 39.35  E-value: 2.65e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 597837628   657 PHPNDATRYLQCTPmigrrGRWTERMCPPNLVFIPSYGRC 696
Cdd:smart00494  12 PHPTDCSKYYQCSN-----GRPIVGSCPAGLVFNPATQTC 46
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
257-464 2.66e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.12  E-value: 2.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 257 NAEMEQLERQ---RQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEWQREIA 333
Cdd:COG4372  107 QEEAEELQEEleeLQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALD 186
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 334 RQkaemdEKEKQRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVERKKQEEVRRIEKARKKSEM 413
Cdd:COG4372  187 EL-----LKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIE 261
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 597837628 414 EKKERERQQEIARQHAERQRKEEEARRQEEARLFAERQKKERERQEEIARQ 464
Cdd:COG4372  262 ELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGA 312
CCDC47 pfam07946
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ...
357-422 2.68e-04

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


Pssm-ID: 462322  Cd Length: 323  Bit Score: 44.10  E-value: 2.68e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  357 RQRQEEELLRQQEVALQEAERQKKErerqkeiarqvvERKKQEEVRRIEK----ARKKseMEKKERERQQ 422
Cdd:pfam07946 266 REEEIEKIKKAAEEERAEEAQEKKE------------EAKKKEREEKLAKlspeEQRK--YEEKERKKEQ 321
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
257-366 2.74e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.76  E-value: 2.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 257 NAEMEQLE--RQRQQEIARQVAERQQKEREELEWQQEIARQEAE-RQRKEEEMRR-QQEYAQQMAEMQRAQKEME-WQRE 331
Cdd:COG4717  142 AELPERLEelEERLEELRELEEELEELEAELAELQEELEELLEQlSLATEEELQDlAEELEELQQRLAELEEELEeAQEE 221
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 597837628 332 IARQKAEMDEKEKQRQVEiarQMAERQRQEEELLR 366
Cdd:COG4717  222 LEELEEELEQLENELEAA---ALEERLKEARLLLL 253
DDRGK pfam09756
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ...
333-417 2.94e-04

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


Pssm-ID: 370664 [Multi-domain]  Cd Length: 188  Bit Score: 42.72  E-value: 2.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  333 ARQKAEMDEKEKQRQ----VEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQvvERKKQEEVRRIekar 408
Cdd:pfam09756   5 AKKRAKLELKEAKRQqreaEEEEREEREKLEEKREEEYKEREEREEEAEKEKEEEERKQEEEQ--ERKEQEEYEKL---- 78

                  ....*....
gi 597837628  409 kKSEMEKKE 417
Cdd:pfam09756  79 -KSQFVVEE 86
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
245-521 3.16e-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: 3.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   245 QGPSGNFEEGSSNAEMEQLERQRQQEIARQVAERQQKEREELEWQQEIARQEAE------RQRKEEEMRRQQEYAQQMAE 318
Cdd:TIGR00618  151 QGEFAQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQlltlctPCMPDTYHERKQVLEKELKH 230
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   319 MQRAQKEMEWQREIARQKAEMDEKEKQRQveiarQMAERQRQEEELLRQQEVALqeaERQKKERERQKEIARQVVERKKQ 398
Cdd:TIGR00618  231 LREALQQTQQSHAYLTQKREAQEEQLKKQ-----QLLKQLRARIEELRAQEAVL---EETQERINRARKAAPLAAHIKAV 302
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   399 EEVRriekarkksemekkererqQEIARQHAERQRKEEEARRQEEARLFAERQKKERERQEEIARQMEEEEKRQREEAEK 478
Cdd:TIGR00618  303 TQIE-------------------QQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEV 363
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 597837628   479 EEMRKRKIEEERLRKEEEQRIEAQRKAEEERrieEQLAAREVE 521
Cdd:TIGR00618  364 ATSIREISCQQHTLTQHIHTLQQQKTTLTQK---LQSLCKELD 403
fliH PRK06669
flagellar assembly protein H; Validated
262-419 3.53e-04

flagellar assembly protein H; Validated


Pssm-ID: 235850 [Multi-domain]  Cd Length: 281  Bit Score: 43.47  E-value: 3.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 262 QLERQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQMAeMQRAQKEMEWQREIARQKAEmde 341
Cdd:PRK06669  13 NKEKLKTHEIQKYRFKVLSIKEKERLREEEEEQVEQLREEANDEAKEIIEEAEEDA-FEIVEAAEEEAKEELLKKTD--- 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 342 kEKQRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVERKKQEEVRRIEKARKKSE--MEKKERE 419
Cdd:PRK06669  89 -EASSIIEKLQMQIEREQEEWEEELERLIEEAKAEGYEEGYEKGREEGLEEVRELIEQLNKIIEKLIKKREeiLESSEEE 167
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
292-515 3.90e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.14  E-value: 3.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  292 IARQEAERQRKEEEMRRQQEyaqQMAEMQRAQKEMEWQREIARQKAEMDEKE---KQRQVEIARQMAERQRqeeelLRQQ 368
Cdd:COG4913   612 LAALEAELAELEEELAEAEE---RLEALEAELDALQERREALQRLAEYSWDEidvASAEREIAELEAELER-----LDAS 683
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  369 EVALQEAERQKKERERQKEIARQvverkkqeevrRIEKARKKSEMEKKERERQQEIARQHAERQRKEEEARRQEEARLFA 448
Cdd:COG4913   684 SDDLAALEEQLEELEAELEELEE-----------ELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLE 752
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 597837628  449 ERqkKERERQEEIARQMEEEekrqreeaekeemrkrkieeerlrkeeeqrIEAQRKAEEER--RIEEQL 515
Cdd:COG4913   753 ER--FAAALGDAVERELREN------------------------------LEERIDALRARlnRAEEEL 789
PRK07735 PRK07735
NADH-quinone oxidoreductase subunit C;
266-418 3.99e-04

NADH-quinone oxidoreductase subunit C;


Pssm-ID: 236081 [Multi-domain]  Cd Length: 430  Bit Score: 43.82  E-value: 3.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 266 QRQQEIARQvAERQQKEREELEWQQEIARQEAERQRKE------------EEMRRQQEYAQQMAEMQRAQKEMEWQR--- 330
Cdd:PRK07735   9 DLKKEAARR-AKEEARKRLVAKHGAEISKLEEENREKEkalpknddmtieEAKRRAAAAAKAKAAALAKQKREGTEEvte 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 331 -EIARQKAEMDEKEKQRQVEIARQ--MAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQvvERKKQEEVRRIEKA 407
Cdd:PRK07735  88 eEKAKAKAKAAAAAKAKAAALAKQkrEGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTE--EVTEEEEETDKEKA 165
                        170
                 ....*....|.
gi 597837628 408 RKKSEMEKKER 418
Cdd:PRK07735 166 KAKAAAAAKAK 176
Pinin_SDK_memA pfam04696
pinin/SDK/memA/ protein conserved region; Members of this family have very varied ...
255-330 4.36e-04

pinin/SDK/memA/ protein conserved region; Members of this family have very varied localizations within the eukaryotic cell. pinin is known to localize at the desmosomes and is implicated in anchoring intermediate filaments to the desmosomal plaque. SDK2/3 is a dynamically localized nuclear protein thought to be involved in modulation of alternative pre-mRNA splicing. memA is a tumour marker preferentially expressed in human melanoma cell lines. A common feature of the members of this family is that they may all participate in regulating protein-protein interactions.


Pssm-ID: 461396 [Multi-domain]  Cd Length: 130  Bit Score: 41.12  E-value: 4.36e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 597837628  255 SSNAEMEQLERQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEemrrQQEYAQQMAEMQRAQKEMEWQR 330
Cdd:pfam04696  22 KKEESKQKEKEERRAEIEKRLEEKAKQEKEELEERKREEREELFEERRAE----QIELRALEEKLELKELMETWHE 93
PRK07352 PRK07352
F0F1 ATP synthase subunit B; Validated
263-382 4.45e-04

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 180941 [Multi-domain]  Cd Length: 174  Bit Score: 41.86  E-value: 4.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 263 LERqRQQEIA---RQVAERQQKEREELEWQQE---IARQEAERQRKEeemrrqqeyAQQMAEMQRAQKEMEWQREIAR-- 334
Cdd:PRK07352  48 LEE-RREAILqalKEAEERLRQAAQALAEAQQklaQAQQEAERIRAD---------AKARAEAIRAEIEKQAIEDMARlk 117
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 597837628 335 QKAEMDEKekqrqveiarqmAERQRQEEELLRQ-QEVALQEAERQKKER 382
Cdd:PRK07352 118 QTAAADLS------------AEQERVIAQLRREaAELAIAKAESQLPGR 154
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
290-420 4.46e-04

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: 41.98  E-value: 4.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  290 QEIARQEAERQRKEEEmrRQQEYAQQMAEMQRAQKEMEWQREIARQKAEMDEKEKQRQVEIARQMAERQRQEEELLRQQE 369
Cdd:pfam11600   4 QKSVQSQEEKEKQRLE--KDKERLRRQLKLEAEKEEKERLKEEAKAEKERAKEEARRKKEEEKELKEKERREKKEKDEKE 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 597837628  370 VALQEAERQKKERERQKEIARQVVERKKQEEVRRIEKARKKSEMEKKERER 420
Cdd:pfam11600  82 KAEKLRLKEEKRKEKQEALEAKLEEKRKKEEEKRLKEEEKRIKAEKAEITR 132
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
257-461 4.61e-04

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 43.36  E-value: 4.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 257 NAEMEQLeRQRQQEIARQVAERQQKEREELEWQQEIARQEAERQ----RKEEEMRRQQEYAQQMAEMQRAQKEMEWQREI 332
Cdd:COG1340   84 NEKLNEL-REELDELRKELAELNKAGGSIDKLRKEIERLEWRQQtevlSPEEEKELVEKIKELEKELEKAKKALEKNEKL 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 333 ARQKAEMDEKEKQRQvEIARQMAERQRQEEELLRQQEVALQEAERQKKERErqkEIARQVVErkKQEEVRRIEKarKKSE 412
Cdd:COG1340  163 KELRAELKELRKEAE-EIHKKIKELAEEAQELHEEMIELYKEADELRKEAD---ELHKEIVE--AQEKADELHE--EIIE 234
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 597837628 413 MEKKERERQQEIARQHAERQRKEEearrqeearlfAERQKKERERQEEI 461
Cdd:COG1340  235 LQKELRELRKELKKLRKKQRALKR-----------EKEKEELEEKAEEI 272
RIB43A pfam05914
RIB43A; This family consists of several RIB43A-like eukaryotic proteins. Ciliary and flagellar ...
263-460 4.74e-04

RIB43A; This family consists of several RIB43A-like eukaryotic proteins. Ciliary and flagellar microtubules contain a specialized set of protofilaments, termed ribbons, that are composed of tubulin and several associated proteins. RIB43A was first characterized in the unicellular biflagellate, Chlamydomonas reinhardtii although highly related sequences are present in several higher eukaryotes including humans. The function of this protein is unknown although the structure of RIB43A and its association with the specialized protofilament ribbons and with basal bodies is relevant to the proposed role of ribbons in forming and stabilising doublet and triplet microtubules and in organizing their three-dimensional structure. Human RIB43A homologs could represent a structural requirement in centriole replication in dividing cells.


Pssm-ID: 461780 [Multi-domain]  Cd Length: 372  Bit Score: 43.35  E-value: 4.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  263 LERQRQQEIARQ----------------VAERQQKEREElewqqeiaRQEAERQRKE---EEMRRQQEYAQQM-AEMQRA 322
Cdd:pfam05914   9 IERRRQREEERKsrifnarnrtigvdveALDKQVEEKKR--------QEAAEKAREEafaEEMVQNDKIALMLeKREEED 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  323 QKEME------WQREiarQKAEM---------DEKEKQRQVEIARQ------------MAERQRQEEELLRQQEVALQEA 375
Cdd:pfam05914  81 RRRLNkelnefRQQH---QRPETrrefdlndpDALKKDLPARVSDDdprcgpssmqkfEGEDLNREERKKLQQEQMREWL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  376 ERQKKERERQKEIARQvveRKKQEEVRRIEKARKKSEMEKKERERQQEIAR--------QHAERqrkeeearrqeearlf 447
Cdd:pfam05914 158 EQQIEEKKQAEEEEKH---AELLYDQKRLERDRRALELAKLEEECRRAVNAatknfnqaLAAEQ---------------- 218
                         250
                  ....*....|...
gi 597837628  448 AERQKKERERQEE 460
Cdd:pfam05914 219 AERRRLEKRQEQE 231
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
258-432 4.81e-04

Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.


Pssm-ID: 437057 [Multi-domain]  Cd Length: 401  Bit Score: 43.52  E-value: 4.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  258 AEMEQLERQRQQEI--ARQVAERQQKEREELEwQQEIARQEAERQRK---------EEEMRRQQ----EYAQQMAEMQRA 322
Cdd:pfam19220 118 AQAEALERQLAAETeqNRALEEENKALREEAQ-AAEKALQRAEGELAtarerlallEQENRRLQalseEQAAELAELTRR 196
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  323 QKEMEWQREIARQKAEMDEkekqrqVEIARQMAERQRQEEELLrqQEVALQEAERQKKERERQKEIAR---------QVV 393
Cdd:pfam19220 197 LAELETQLDATRARLRALE------GQLAAEQAERERAEAQLE--EAVEAHRAERASLRMKLEALTARaaateqllaEAR 268
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 597837628  394 E--RKKQEEVRRIEKARKKSEMEKKERERQQEIARQHAERQ 432
Cdd:pfam19220 269 NqlRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERR 309
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
308-404 5.29e-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: 41.31  E-value: 5.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 308 RQQEYAQQMAEMQRAQKEMEWQREIARQKAEMDEKEKQRQVEIARQMAERQRQEeellrqqevALQEAErqkKERERQKE 387
Cdd:COG0711   32 RQEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARKEAEAIAEE---------AKAEAE---AEAERIIA 99
                         90       100
                 ....*....|....*....|
gi 597837628 388 IARQVVERKKQ---EEVRRI 404
Cdd:COG0711  100 QAEAEIEQERAkalAELRAE 119
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
257-332 5.35e-04

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: 41.75  E-value: 5.35e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 597837628 257 NAEMEQLERQRQQEIARQVAERQQKErEELEwQQEIARQEAERQRKEEE-MRRQQEYAQQMAEMQR--AQKEMEWQREI 332
Cdd:COG2825   45 QKKLEKEFKKRQAELQKLEKELQALQ-EKLQ-KEAATLSEEERQKKERElQKKQQELQRKQQEAQQdlQKRQQELLQPI 121
KASH_CCD pfam14662
Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of ...
253-414 5.45e-04

Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of KASH or Klarsicht/ANC-1/Syne/homology proteins. KASH are a meiosis-specific proteins that localize at telomeres and interact with SUN1, thus being implicated in meiotic chromosome dynamics and homolog pairing.


Pssm-ID: 405365 [Multi-domain]  Cd Length: 191  Bit Score: 42.09  E-value: 5.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  253 EGSSNAEMEQLERQRQQEIARQVAERQQKE-REELEWQQEIARQEAERQRKEEEMRRQQEYAQQmaemQRAQKEMEWQRE 331
Cdd:pfam14662  35 EETNAKLLEENLNLRKQAKSQQQAVQKEKLlEEELEDLKLIVNSLEEARRSLLAQNKQLEKENQ----SLLQEIESLQEE 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  332 IARQKAEMDEKEKQRQvEIARQMAERQRQEEELlrqQEVALQEAERQKKERERQKEIARQVVERKKQEEVRRIEKARKKS 411
Cdd:pfam14662 111 NKKNQAERDKLQKKKK-ELLKSKACLKEQLHSC---EDLACNRETILIEKTTQIEELKSTVEEYSSIEEELRAEKSRLES 186

                  ...
gi 597837628  412 EME 414
Cdd:pfam14662 187 QLP 189
EVC2_like pfam12297
Ellis van Creveld protein 2 like protein; This family of proteins is found in eukaryotes. ...
261-421 5.96e-04

Ellis van Creveld protein 2 like protein; This family of proteins is found in eukaryotes. Proteins in this family are typically between 571 and 1310 amino acids in length. There are two conserved sequence motifs: LPA and ELH. EVC2 is implicated in Ellis van Creveld chondrodysplastic dwarfism in humans. Mutations in this protein can give rise to this congenital condition. LIMBIN is a protein which shares around 80% sequence homology with EVC2 and it is implicated in a similar condition in bovine chondrodysplastic dwarfism.


Pssm-ID: 463525 [Multi-domain]  Cd Length: 428  Bit Score: 43.15  E-value: 5.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  261 EQLERQRQQEIARQVAERQQKEREELEWQQEiaRQEAERQRKEEEMRR--QQEYAQ--QMAEMQRAQKEMEWQREIARQK 336
Cdd:pfam12297 209 GRLQEEYERKMAALAAECNLETREKMEAQHQ--REMAEKEEAEELLKHadEQEALEcsSLLDKLHKLEQEHLQRSLLLRQ 286
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  337 AEMDEKekqrqveIARQMAERQRQEeeLLRQQEVALQEAERQKkerERQKEIARQVVERKKQ-----EEVRRIEKARKKS 411
Cdd:pfam12297 287 EEDFAK-------AQRQLAVFQRVE--LHKIFFTQLKEATRKG---ELKPEAAKRLLQDYSKiqeqiEELMDFFQANQRY 354
                         170
                  ....*....|
gi 597837628  412 EMEKKERERQ 421
Cdd:pfam12297 355 HLSERFAQRE 364
PRK14474 PRK14474
F0F1 ATP synthase subunit B; Provisional
262-393 6.08e-04

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 184696 [Multi-domain]  Cd Length: 250  Bit Score: 42.50  E-value: 6.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 262 QLERQRQQEIARQVAERQQkereelewQQEIARQEAERQRKEeemrrQQEYAQQMAEMqraqkemewqreIARQKAEMDE 341
Cdd:PRK14474  32 QVMKKRQQRIANRWQDAEQ--------RQQEAGQEAERYRQK-----QQSLEQQRASF------------MAQAQEAADE 86
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 597837628 342 kEKQRQVEIARQMAERQRQE--EELLRQQEVALQEAerQKKERERQKEIARQVV 393
Cdd:PRK14474  87 -QRQHLLNEAREDVATARDEwlEQLEREKQEFFKAL--QQQTGQQMVKIIRAAL 137
ATP-synt_B pfam00430
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is ...
308-395 6.24e-04

ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is thought to translocate protons through membrane (inner membrane in mitochondria, thylakoid membrane in plants, cytoplasmic membrane in bacteria). The B subunits are thought to interact with the stalk of the CF(1) subunits. This domain should not be confused with the ab CF(1) proteins (in the head of the ATP synthase) which are found in pfam00006


Pssm-ID: 425677 [Multi-domain]  Cd Length: 132  Bit Score: 40.76  E-value: 6.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  308 RQQEYAQQMAEMQRAQKEMEWQREIARQKAEMDEKEKQRQVEIARQMAERQRQE------EELLRQQEVALQEAERQKKE 381
Cdd:pfam00430  31 RRELIADEIAEAEERRKDAAAALAEAEQQLKEARAEAQEIIENAKKRAEKLKEEivaaaeAEAERIIEQAAAEIEQEKDR 110
                          90
                  ....*....|....*....
gi 597837628  382 -----RERQKEIARQVVER 395
Cdd:pfam00430 111 alaelRQQVVALAVQIAEK 129
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
198-521 6.76e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.51  E-value: 6.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 198 EDEFLKQLVRIVEAHQVAINKIEEQVGEERRRGGVEDHEHPAGSFRKqgpsgnfEEGSSNAEMEQLErqrqqEIARQVAE 277
Cdd:PRK03918 199 EKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEK-------ELESLEGSKRKLE-----EKIRELEE 266
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 278 RQQKEREELEWQQEIARQEAERQRKEEEMRR-QQEYAQQMAEMQRAQKEME-WQREIARQKAEMDEKE-KQRQVEIARQM 354
Cdd:PRK03918 267 RIEELKKEIEELEEKVKELKELKEKAEEYIKlSEFYEEYLDELREIEKRLSrLEEEINGIEERIKELEeKEERLEELKKK 346
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 355 AERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVERKKQEEVRRIEKARKKSEMEKKE-RERQQEIARQHAERQR 433
Cdd:PRK03918 347 LKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKiTARIGELKKEIKELKK 426
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 434 KEEEARRQEEARLFAERQKKERERQEEIARQMEE----EEKRQREEAEKEEMRKRKIEEERLRKEEEQRIEAQRKAEEER 509
Cdd:PRK03918 427 AIEELKKAKGKCPVCGRELTEEHRKELLEEYTAElkriEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLK 506
                        330
                 ....*....|..
gi 597837628 510 RIEEQLAAREVE 521
Cdd:PRK03918 507 ELEEKLKKYNLE 518
DivIVA COG3599
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle ...
277-360 6.95e-04

Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442818 [Multi-domain]  Cd Length: 125  Bit Score: 40.22  E-value: 6.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 277 ERQQKEREELEWQQEIARQEAERQRK-EEEMRRQQEYAQQMAEMQR--AQKEMEWQREIARQKAE-MDEKEKQRQVEIAR 352
Cdd:COG3599   37 ERLIRENKELKEKLEELEEELEEYRElEETLQKTLVVAQETAEEVKenAEKEAELIIKEAELEAEkIIEEAQEKARKIVR 116

                 ....*...
gi 597837628 353 QMAERQRQ 360
Cdd:COG3599  117 EIEELKRQ 124
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
264-419 7.62e-04

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


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 42.96  E-value: 7.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  264 ERQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEWQREIARQKAEMdeke 343
Cdd:pfam07888  38 ECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEEL---- 113
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 597837628  344 KQRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVERKKQEEVrriEKARKKSEMEKKERE 419
Cdd:pfam07888 114 SEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEA---ERKQLQAKLQQTEEE 186
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
197-523 7.82e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.39  E-value: 7.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 197 SEDEFLKQLVRIVEAHQVAINKIEEQVGEERRRGGvEDHEHPAGSFRKQGPSGNFEEGSSNAEMEQLERQRQQEIARQVA 276
Cdd:COG1196  380 ELEELAEELLEALRAAAELAAQLEELEEAEEALLE-RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE 458
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 277 ERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEW--------QREIARQKAEMDEKEK---- 344
Cdd:COG1196  459 EALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVkaalllagLRGLAGAVAVLIGVEAayea 538
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 345 -------QRQVEIARQMAERQRQEEELLRQQE---VALQEAERQKKERERQKEIARQVVERK------------------ 396
Cdd:COG1196  539 aleaalaAALQNIVVEDDEVAAAAIEYLKAAKagrATFLPLDKIRARAALAAALARGAIGAAvdlvasdlreadaryyvl 618
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 397 -KQEEVRRIEKARKKSEMEKKERERQQEIARQHAERQRKEEEARRQEEARLFAERQKKERERQEEIARQMEEEEKRQREE 475
Cdd:COG1196  619 gDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEA 698
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 597837628 476 AEKEEMRKRKIeeerlrKEEEQRIEAQRKAEEERRIEEQLAAREVENQ 523
Cdd:COG1196  699 LLAEEEEEREL------AEAEEERLEEELEEEALEEQLEAEREELLEE 740
Caldesmon pfam02029
Caldesmon;
220-413 8.02e-04

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 42.93  E-value: 8.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  220 EEQVGEERRRGGVEDHEHPAGSFRKQGPSGNFEEGSSNAEMEQLERQRQQEIARQVAERQQ----KEREELE-------- 287
Cdd:pfam02029 118 EEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEVPTENFAKEEvkdeKIKKEKKvkyeskvf 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  288 WQQEIARQEAERQRKEEE----------MRRQQEYAQQMAEMQRAQKEMEWQRE-IARQKAEMDEKE----KQRQVEIAR 352
Cdd:pfam02029 198 LDQKRGHPEVKSQNGEEEvtklkvttkrRQGGLSQSQEREEEAEVFLEAEQKLEeLRRRRQEKESEEfeklRQKQQEAEL 277
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 597837628  353 QMAERQRQEEELLRqqevALQEAERQKKERERQKEIARQVVERKKQEEV--RRIEKARKKSEM 413
Cdd:pfam02029 278 ELEELKKKREERRK----LLEEEEQRRKQEEAERKLREEEEKRRMKEEIerRRAEAAEKRQKL 336
Spb1_C pfam07780
Spb1 C-terminal domain; This presumed domain is found at the C-terminus of a family of ...
382-426 8.21e-04

Spb1 C-terminal domain; This presumed domain is found at the C-terminus of a family of FtsJ-like methyltransferases. Members of this family are involved in 60S ribosomal biogenesis, for example Swiss:P25582.


Pssm-ID: 462264  Cd Length: 209  Bit Score: 41.83  E-value: 8.21e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 597837628  382 RERQKEI-AR---QVVE---RKKQEEVRRIEKARKKSEM-----EKKERERQQEIAR 426
Cdd:pfam07780  97 KEKLRALnARpikKVAEakaRKKMRAAKRLEKAKKKAELinedeDMSEREKAKQIEK 153
Lipase_chap pfam03280
Proteobacterial lipase chaperone protein;
263-383 8.40e-04

Proteobacterial lipase chaperone protein;


Pssm-ID: 427230 [Multi-domain]  Cd Length: 185  Bit Score: 41.14  E-value: 8.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  263 LERQR-QQEIARQVAERQQKereeleWQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQ---------RAQKEMEWQREI 332
Cdd:pfam03280  64 LERLAiAQDSALSAEEKQQR------LAALRAQLPEDLRAAREAQQRLQELAARTAQLQkagaspqqlRQARAQLVGPEA 137
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 597837628  333 ARQKAEMDEKEKQRQVEIARQMAERQRQEEEllrqqevALQEAERQKKERE 383
Cdd:pfam03280 138 AQRLAALDQQRAAWQQRLDDYLAERQQINAA-------GLSEQERQAAIAQ 181
PRK09039 PRK09039
peptidoglycan -binding protein;
258-381 8.71e-04

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 42.65  E-value: 8.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 258 AEMEQLERQRQQEIARQVAERQ------QKEREELE-WQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEM---- 326
Cdd:PRK09039  66 ADLLSLERQGNQDLQDSVANLRaslsaaEAERSRLQaLLAELAGAGAAAEGRAGELAQELDSEKQVSARALAQVELlnqq 145
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 597837628 327 --EWQREIARQKAEMDEKEKQRQveiarqmaERQRQEEELLRQQEVAL----QEAERQKKE 381
Cdd:PRK09039 146 iaALRRQLAALEAALDASEKRDR--------ESQAKIADLGRRLNVALaqrvQELNRYRSE 198
PRK10927 PRK10927
cell division protein FtsN;
261-398 8.87e-04

cell division protein FtsN;


Pssm-ID: 236797 [Multi-domain]  Cd Length: 319  Bit Score: 42.36  E-value: 8.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 261 EQLERQRQQEIARQVAERQQKERE--ELEWQQEIARQeaeRQRKEEEMRRQQEYAQ-QMAEMQRAQKEMEWQReiarQKA 337
Cdd:PRK10927 112 EQLTPEQRQLLEQMQADMRQQPTQlvEVPWNEQTPEQ---RQQTLQRQRQAQQLAEqQRLAQQSRTTEQSWQQ----QTR 184
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 597837628 338 EMDEKEKQRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVERKKQ 398
Cdd:PRK10927 185 TSQAAPVQAQPRQSKPASTQQPYQDLLQTPAHTTAQSKPQQAAPVTRAADAPKPTAEKKDE 245
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
283-426 9.21e-04

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 41.43  E-value: 9.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  283 REELEWQQEIARQEAERQRKEEEMRR-----QQEYAQQMAEMQRAQKEmewqREIARQKAEMDEKEKQRQVEIARQMAER 357
Cdd:pfam13851  22 RNNLELIKSLKEEIAELKKKEERNEKlmseiQQENKRLTEPLQKAQEE----VEELRKQLENYEKDKQSLKNLKARLKVL 97
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 597837628  358 QRQEEELLRQQEVALQEAERQKKER----ERQKEIARQVVERKKQEEV---RRIEKARKksEMEKKERERQQEIAR 426
Cdd:pfam13851  98 EKELKDLKWEHEVLEQRFEKVERERdelyDKFEAAIQDVQQKTGLKNLlleKKLQALGE--TLEKKEAQLNEVLAA 171
DUF724 pfam05266
Protein of unknown function (DUF724); This family contains several uncharacterized proteins ...
283-343 9.53e-04

Protein of unknown function (DUF724); This family contains several uncharacterized proteins found in Arabidopsis thaliana and other plants. This region is often found associated with Agenet domains and may contain coiled-coil.


Pssm-ID: 428400 [Multi-domain]  Cd Length: 188  Bit Score: 41.11  E-value: 9.53e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 597837628  283 REELEWQQEiARQEAERQRKEEEMRRqQEYAQQMAEMQRAQKEMEWQREIARQKAEMDEKE 343
Cdd:pfam05266 101 KDRQTKLLE-ELKKLEKKIAEEESEK-RKLEEEIDELEKKILELERQLALAKEKKEAADKE 159
PRK03963 PRK03963
V-type ATP synthase subunit E; Provisional
269-369 1.02e-03

V-type ATP synthase subunit E; Provisional


Pssm-ID: 167649 [Multi-domain]  Cd Length: 198  Bit Score: 41.28  E-value: 1.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 269 QEIARQvAERqqkereELEWQQEIARQEAERQrKEEEMRRQQEYAQQMAEMQRAQKEMEWQREIARQKAEMDEKEKQRQV 348
Cdd:PRK03963   9 QEINRE-AEQ------KIEYILEEAQKEAEKI-KEEARKRAESKAEWILRKAKTQAELEKQRIIANAKLEVRRKRLAVQE 80
                         90       100
                 ....*....|....*....|.
gi 597837628 349 EIARQMAERQRQEEELLRQQE 369
Cdd:PRK03963  81 ELISEVLEAVRERLAELPEDE 101
PRK07735 PRK07735
NADH-quinone oxidoreductase subunit C;
323-518 1.04e-03

NADH-quinone oxidoreductase subunit C;


Pssm-ID: 236081 [Multi-domain]  Cd Length: 430  Bit Score: 42.66  E-value: 1.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 323 QKEMEWQREIARQKAEMDEKEK---QRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVERKKQE 399
Cdd:PRK07735   4 EKDLEDLKKEAARRAKEEARKRlvaKHGAEISKLEEENREKEKALPKNDDMTIEEAKRRAAAAAKAKAAALAKQKREGTE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 400 EVRRIEKARKKSEMEKKERERQQEIARQHAERQRKEEEARRQEEARLFAERQKKERERQEEIARQMEEEEKRQREEAEKE 479
Cdd:PRK07735  84 EVTEEEKAKAKAKAAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTEEEEETDKE 163
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 597837628 480 EMRKRKIEEERLRKEEEQRIEAQRKAEEERRIEEQLAAR 518
Cdd:PRK07735 164 KAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEKAK 202
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
280-364 1.11e-03

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


Pssm-ID: 464003 [Multi-domain]  Cd Length: 119  Bit Score: 39.47  E-value: 1.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  280 QKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQ--------KEMEWQREIARQKAEMDEKEKQR----- 346
Cdd:pfam13863   3 EKKREMFLVQLALDAKREEIERLEELLKQREEELEKKEQELKEDlikfdkflKENDAKRRRALKKAEEETKLKKEkekei 82
                          90       100
                  ....*....|....*....|.
gi 597837628  347 ---QVEIARQMAERQRQEEEL 364
Cdd:pfam13863  83 kklTAQIEELKSEISKLEEKL 103
PRK12705 PRK12705
hypothetical protein; Provisional
258-398 1.12e-03

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 42.39  E-value: 1.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 258 AEMEQLERQRQQEIARQVAERQQKEREELEWQQEIARQEAER-----QRKEEEMRRQQEYAQQMAEMQRAQKE--MEWQR 330
Cdd:PRK12705  33 KEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARRereelQREEERLVQKEEQLDARAEKLDNLENqlEEREK 112
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 597837628 331 EIARQKAEMDEKEKQRQ---VEIARQMAERQRQeeELLRQQEvalQEAERQKKER-ERQKEIARQVVERKKQ 398
Cdd:PRK12705 113 ALSARELELEELEKQLDnelYRVAGLTPEQARK--LLLKLLD---AELEEEKAQRvKKIEEEADLEAERKAQ 179
YscO pfam07321
Type III secretion protein YscO; This family contains the bacterial type III secretion protein ...
265-414 1.14e-03

Type III secretion protein YscO; This family contains the bacterial type III secretion protein YscO, which is approximately 150 residues long. YscO has been shown to be required for high-level expression and secretion of the anti-host proteins V antigen and Yops in Yersinia pestis.


Pssm-ID: 399954 [Multi-domain]  Cd Length: 148  Bit Score: 40.46  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  265 RQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEWQREIarqkAEMDEKEK 344
Cdd:pfam07321   8 KHLREDRAEKAVKRQEQALAAARAAHQQAQASLQDYRAWRPQEEQRLYAEIQGKLVLLKELEKVKQQV----ALLRENEA 83
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  345 QRQVEIArQMAERQRQEEELLRQQEVALQEAERQKkerERQKEIARQVverkkQEEVRRIEKARKKSEME 414
Cdd:pfam07321  84 DLEKQVA-EARQQLEAEREALRQARQALAEARRAV---EKFAELVRLV-----QAEELRQQERQEEQELE 144
PRK12678 PRK12678
transcription termination factor Rho; Provisional
225-457 1.31e-03

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 42.58  E-value: 1.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 225 EERRRGG-VEDHEHPAGSFRKQGPSGNFEEGSSNAEMEQLERQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKE 303
Cdd:PRK12678  56 KEARGGGaAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGE 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 304 EEMRRQQEYAQQMAEmqraqkemewqreiaRQKAEMDEKEKQRQVEIARQMAERQRQEEEllRQQEVALQEAERQKKERE 383
Cdd:PRK12678 136 AARRGAARKAGEGGE---------------QPATEARADAAERTEEEERDERRRRGDRED--RQAEAERGERGRREERGR 198
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 597837628 384 RQKEIARQVVERKKQEEVRRIEKARKKSEMEKKERERQQEIARQHAERQRKEEEARRQEEarlFAERQKKERER 457
Cdd:PRK12678 199 DGDDRDRRDRREQGDRREERGRRDGGDRRGRRRRRDRRDARGDDNREDRGDRDGDDGEGR---GGRRGRRFRDR 269
PRK07735 PRK07735
NADH-quinone oxidoreductase subunit C;
215-391 1.34e-03

NADH-quinone oxidoreductase subunit C;


Pssm-ID: 236081 [Multi-domain]  Cd Length: 430  Bit Score: 42.27  E-value: 1.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 215 AINKIEEQVGEERRRGGVEDHEHPAGSFRKQGPSGNfeEGSSNAEMEQLERQRQQEIARQVAERQQKEREELEWQQEIAR 294
Cdd:PRK07735  47 ALPKNDDMTIEEAKRRAAAAAKAKAAALAKQKREGT--EEVTEEEKAKAKAKAAAAAKAKAAALAKQKREGTEEVTEEEK 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 295 QEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEWQREIARQKAEMDEKEKQRQVEIARQMAERQRQEEELLRQQEVALQE 374
Cdd:PRK07735 125 AAAKAKAAAAAKAKAAALAKQKREGTEEVTEEEEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEKAKAK 204
                        170
                 ....*....|....*..
gi 597837628 375 AERQKKERERQKEIARQ 391
Cdd:PRK07735 205 AKAAAAAKAKAAALAKQ 221
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
299-517 1.42e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.35  E-value: 1.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   299 RQRKEEEMRRQQEYAQQMAEMQRAQKEMEwqreiaRQKaemdeKEKQRQVEIARQMAERQRQEEELlrQQEVALQEAERQ 378
Cdd:TIGR02168  171 KERRKETERKLERTRENLDRLEDILNELE------RQL-----KSLERQAEKAERYKELKAELREL--ELALLVLRLEEL 237
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   379 KKERERQKEIARQVVER---------KKQEEVRRIEKArkKSEMEKKERERQ-------QEIAR--QHAERQRKEEEARR 440
Cdd:TIGR02168  238 REELEELQEELKEAEEEleeltaelqELEEKLEELRLE--VSELEEEIEELQkelyalaNEISRleQQKQILRERLANLE 315
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   441 QEEARLFAERQKKERERQEEIARQMEEEEKRQREEAEKEEMRKRKIEEERLRKEEEQRIEAQRKAEEERR-----IEEQL 515
Cdd:TIGR02168  316 RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRskvaqLELQI 395

                   ..
gi 597837628   516 AA 517
Cdd:TIGR02168  396 AS 397
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
253-431 1.47e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 42.63  E-value: 1.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  253 EGSSNAEMEQLeRQRQQEIARQVAERQQKEREelewQQEIARQEAERQrkeEEMRRQQEYAQQMAE---MQRAQkEMEWQ 329
Cdd:COG3096   831 APDPEAELAAL-RQRRSELERELAQHRAQEQQ----LRQQLDQLKEQL---QLLNKLLPQANLLADetlADRLE-ELREE 901
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  330 REIARQ-KAEMDEKEKQ-RQVEIARQMAERQRQEEELLRQQevaLQEAERQKKERERQKEIARQVVERKK----QEEVRR 403
Cdd:COG3096   902 LDAAQEaQAFIQQHGKAlAQLEPLVAVLQSDPEQFEQLQAD---YLQAKEQQRRLKQQIFALSEVVQRRPhfsyEDAVGL 978
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 597837628  404 I-------EKARKKSEMEKKERERQQEIARQHAER 431
Cdd:COG3096   979 LgensdlnEKLRARLEQAEEARREAREQLRQAQAQ 1013
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
384-517 1.62e-03

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: 41.86  E-value: 1.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  384 RQKEIARQVVERKKQEEVRRIEKARKKSEMEKKERERQQEIAR-QHAERQRKEEEARRQEEARLFAERQKKERERQEEI- 461
Cdd:pfam15709 328 REQEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQEQLERaEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEe 407
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 597837628  462 ARQMEEEEKRQREEAEKEEMRKRKIEEERLRKEEEqriEAQRKAEEERR---IEEQLAA 517
Cdd:pfam15709 408 RKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQE---EAERAEAEKQRqkeLEMQLAE 463
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
258-522 1.75e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.06  E-value: 1.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 258 AEMEQLERQRQQEIAR------QVAERQQKEREELEWQQEIARQEAERQRKEEEM---------RRQQEYAQQMAEMQRA 322
Cdd:COG4717  132 QELEALEAELAELPERleeleeRLEELRELEEELEELEAELAELQEELEELLEQLslateeelqDLAEELEELQQRLAEL 211
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 323 QKEME-WQREIARQKAEMDEKEKQRQVE----------------------------------------------IARQMA 355
Cdd:COG4717  212 EEELEeAQEELEELEEELEQLENELEAAaleerlkearlllliaaallallglggsllsliltiagvlflvlglLALLFL 291
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 356 ERQRQEEELLRQQEVALQEAERQKKERERQKEIARQV-----VERKKQEEVRRIEKARKKSEMEKKERERQQEIARQHAE 430
Cdd:COG4717  292 LLAREKASLGKEAEELQALPALEELEEEELEELLAALglppdLSPEELLELLDRIEELQELLREAEELEEELQLEELEQE 371
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 431 RQRKEEEARRQEEARLFA-----ERQKKERERQEEIARQMEEE---EKRQREEAEKEEMRKRKIEEERLRKEEEQRIEA- 501
Cdd:COG4717  372 IAALLAEAGVEDEEELRAaleqaEEYQELKEELEELEEQLEELlgeLEELLEALDEEELEEELEELEEELEELEEELEEl 451
                        330       340
                 ....*....|....*....|..
gi 597837628 502 -QRKAEEERRIEEQLAAREVEN 522
Cdd:COG4717  452 rEELAELEAELEQLEEDGELAE 473
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
258-380 1.76e-03

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 41.28  E-value: 1.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  258 AEMEQLERQRQQEiARQVAERQQkereelEWQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKeMEWQREIARQKA 337
Cdd:pfam09787  75 TELQELEAQQQEE-AESSREQLQ------ELEEQLATERSARREAEAELERLQEELRYLEEELRRSK-ATLQSRIKDREA 146
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 597837628  338 EMdekEKQRQVEIARQMAERQRQE-EELLRQqevaLQEAERQKK 380
Cdd:pfam09787 147 EI---EKLRNQLTSKSQSSSSQSElENRLHQ----LTETLIQKQ 183
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
269-397 1.78e-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: 40.20  E-value: 1.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 269 QEIARQVAERQQkEREELEwqQEIARQEAERQRKEEEMRrqqeyaqqmAEMQRAQKEmewqreiarqKAEMDEKEKQ-RQ 347
Cdd:COG2825   32 QRILQESPEGKA-AQKKLE--KEFKKRQAELQKLEKELQ---------ALQEKLQKE----------AATLSEEERQkKE 89
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 597837628 348 VEIARQMAERQRQEEEllRQQEVALQEAERQKKERERQKEIARQVVERKK 397
Cdd:COG2825   90 RELQKKQQELQRKQQE--AQQDLQKRQQELLQPILEKIQKAIKEVAKEEG 137
mukB PRK04863
chromosome partition protein MukB;
259-419 1.78e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 42.25  E-value: 1.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  259 EMEQLERQRQQEIARQVAERQQK--------EREELEWQQEIARQEAERQRkEEEMRRQQEYAQQMAEMQRAQ-KEMEWQ 329
Cdd:PRK04863  936 QFEQLKQDYQQAQQTQRDAKQQAfaltevvqRRAHFSYEDAAEMLAKNSDL-NEKLRQRLEQAEQERTRAREQlRQAQAQ 1014
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  330 REIARQ-----KAEMDEKEKQRQvEIARQMAERQRQ----EEELLRQQEVALQEAERQKKERERQKEIARQVVERKKQEE 400
Cdd:PRK04863 1015 LAQYNQvlaslKSSYDAKRQMLQ-ELKQELQDLGVPadsgAEERARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNL 1093
                         170
                  ....*....|....*....
gi 597837628  401 VRRIEKARKKSEMEKKERE 419
Cdd:PRK04863 1094 TKKLRKLERDYHEMREQVV 1112
Caldesmon pfam02029
Caldesmon;
258-522 1.83e-03

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 41.78  E-value: 1.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  258 AEMEQLERQRQQEiARQVAERQQKEREELEWQQEiaRQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEWQREIARQKA 337
Cdd:pfam02029   2 EDEEEAARERRRR-AREERRRQKEEEEPSGQVTE--SVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREERRQKR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  338 EMDEKEKQRQ-----VEIARQMAERQRQEEELlrQQEVALQEAERQKkERERQKEIARQVVERKKQEEVRRIEKARKKSE 412
Cdd:pfam02029  79 LQEALERQKEfdptiADEKESVAERKENNEEE--ENSSWEKEEKRDS-RLGRYKEEETEIREKEYQENKWSTEVRQAEEE 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  413 MEKKEreRQQEIARQHAERQRKEEEARRQEEAR---------LFAERQKKERERQEEIARQMEEEEKRQREEaekeeMRK 483
Cdd:pfam02029 156 GEEEE--DKSEEAEEVPTENFAKEEVKDEKIKKekkvkyeskVFLDQKRGHPEVKSQNGEEEVTKLKVTTKR-----RQG 228
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 597837628  484 RKIEEERLRKEEEQRIEAQRKAEEERRIEEQLAAREVEN 522
Cdd:pfam02029 229 GLSQSQEREEEAEVFLEAEQKLEELRRRRQEKESEEFEK 267
DUF4618 pfam15397
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins ...
261-361 1.89e-03

Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins in this family are typically between 238 and 363 amino acids in length. There are two conserved sequence motifs: EYP and KCTPD.


Pssm-ID: 464704 [Multi-domain]  Cd Length: 258  Bit Score: 41.09  E-value: 1.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  261 EQLERQRQQeiarqVAERQQKEREELE--WQQEIARQEAERQRKEEEM-----RRQQEYAQQmAEMQRAQKEMEWQREIA 333
Cdd:pfam15397 123 ANLVRQLQQ-----LKDSQQDELDELEemRRMVLESLSRKIQKKKEKIlsslaEKTLSPYQE-SLLQKTRDNQVMLKEIE 196
                          90       100       110
                  ....*....|....*....|....*....|...
gi 597837628  334 RQKAEMDEKEK-----QRQVEIARQMAERQRQE 361
Cdd:pfam15397 197 QFREFIDELEEeipklKAEVQQLQAQRQEPREV 229
secA PRK12903
preprotein translocase subunit SecA; Reviewed
252-386 1.97e-03

preprotein translocase subunit SecA; Reviewed


Pssm-ID: 237258 [Multi-domain]  Cd Length: 925  Bit Score: 41.96  E-value: 1.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 252 EEGSSNAEMEQLERQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQ--QEYAQQMAEMQRAQKEmewQ 329
Cdd:PRK12903 788 TEILSDGINNSDINDRPQELIDQIIESEEERLKALRIQREEMLMRPEELELINEEQKNlkQEIKLELSEIQEAEEE---I 864
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 597837628 330 REIARQKAEMDEKEKQ----RQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQK 386
Cdd:PRK12903 865 QNINENKNEFVEFKNDpkklNKLIIAKDVLIKLVISSDEIKQDEKTTKKKKKDLEKTDEEA 925
PRK13428 PRK13428
F0F1 ATP synthase subunit delta; Provisional
306-396 2.06e-03

F0F1 ATP synthase subunit delta; Provisional


Pssm-ID: 184048 [Multi-domain]  Cd Length: 445  Bit Score: 41.64  E-value: 2.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 306 MRRQQEYA-QQMAEMQRAQKEMEwQREIARQKAEMDEK-EKQRQVEIARQMAERQRQEeelLRQQevALQEAERQKKERE 383
Cdd:PRK13428  30 MAARQDTVrQQLAESATAADRLA-EADQAHTKAVEDAKaEAARVVEEAREDAERIAEQ---LRAQ--ADAEAERIKVQGA 103
                         90
                 ....*....|...
gi 597837628 384 RQKEIARQVVERK 396
Cdd:PRK13428 104 RQVQLLRAQLTRQ 116
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
366-431 2.19e-03

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


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 38.96  E-value: 2.19e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 597837628 366 RQQEVA--LQEAERQKKERERQKEIARQVVERKKQEEVRRIEKARKKSEmekKERERQQEIARQHAER 431
Cdd:cd06503   31 REEKIAesLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKEAE---KIKEEILAEAKEEAER 95
CCDC47 pfam07946
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ...
270-347 2.22e-03

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


Pssm-ID: 462322  Cd Length: 323  Bit Score: 41.01  E-value: 2.22e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 597837628  270 EIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEyaQQMAEMQRAQkemewQREIarqkaemDEKEKQRQ 347
Cdd:pfam07946 257 EALKKAKKTREEEIEKIKKAAEEERAEEAQEKKEEAKKKERE--EKLAKLSPEE-----QRKY-------EEKERKKE 320
FliJ pfam02050
Flagellar FliJ protein;
313-427 2.33e-03

Flagellar FliJ protein;


Pssm-ID: 426581 [Multi-domain]  Cd Length: 123  Bit Score: 38.80  E-value: 2.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  313 AQQMAEMQRAQKEMEwqREIARQKAEMDEKEKQRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQV 392
Cdd:pfam02050   4 ARELAEAQRELQQAE--EKLEELQQYRAEYQQQLSGAGQGISAAELRNYQAFISQLDEAIAQQQQELAQAEAQVEKAREE 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 597837628  393 VeRKKQEEVRRIEK--ARKKSEMEKKERERQQ----EIARQ 427
Cdd:pfam02050  82 W-QEARQERKSLEKlrEREKKEERKEQNRREQkqldELAAR 121
PRK07353 PRK07353
F0F1 ATP synthase subunit B'; Validated
294-395 2.47e-03

F0F1 ATP synthase subunit B'; Validated


Pssm-ID: 235999 [Multi-domain]  Cd Length: 140  Bit Score: 39.22  E-value: 2.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 294 RQEAeRQRKEEEMRRQQEYAQQMAEMQR------AQKEMEWQReIARQKAEMDEKEKQRQVEIARQMAERQRQEeellrq 367
Cdd:PRK07353  45 RAEA-KERLAEAEKLEAQYEQQLASARKqaqaviAEAEAEADK-LAAEALAEAQAEAQASKEKARREIEQQKQA------ 116
                         90       100
                 ....*....|....*....|....*...
gi 597837628 368 qevALQEAERQkkererQKEIARQVVER 395
Cdd:PRK07353 117 ---ALAQLEQQ------VDALSRQILEK 135
PKK pfam12474
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino ...
259-386 2.47e-03

Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino acids in length. The family is found in association with pfam00069. Polo-like kinase 1 (Plx1) is essential during mitosis for the activation of Cdc25C, for spindle assembly, and for cyclin B degradation. This family is Polo kinase kinase (PKK) which phosphorylates Polo kinase and Polo-like kinase to activate them. PKK is a serine/threonine kinase.


Pssm-ID: 463600 [Multi-domain]  Cd Length: 139  Bit Score: 39.08  E-value: 2.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  259 EMEQLERQRQQEIARqvAERQQK-EREELEWQQEIA-RQEAERQRKEEEMRrqqeyaqqMAEMQRAQKEmewqrEIARQK 336
Cdd:pfam12474  15 ERQQLKKRYEKELEQ--LERQQKqQIEKLEQRQTQElRRLPKRIRAEQKKR--------LKMFRESLKQ-----EKKELK 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 597837628  337 AEMDEKEKQRQVEIARQMAERQRQEEellRQQEVALQEAERQKKERERQK 386
Cdd:pfam12474  80 QEVEKLPKFQRKEAKRQRKEELELEQ---KHEELEFLQAQSEALERELQQ 126
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
269-374 2.47e-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: 39.10  E-value: 2.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   269 QEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQqeyAQQMAEMQRAQKEmewqREIARQKAEMDEKEKQRQV 348
Cdd:smart00935  11 QESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKD---AATLSEAAREKKE----KELQKKVQEFQRKQQKLQQ 83
                           90       100
                   ....*....|....*....|....*...
gi 597837628   349 EIARQMAERQRQEEELLRQ--QEVALQE 374
Cdd:smart00935  84 DLQKRQQEELQKILDKINKaiKEVAKKK 111
HAUS5 pfam14817
HAUS augmin-like complex subunit 5; This family includes HAUS augmin-like complex subunit 5. ...
268-377 2.61e-03

HAUS augmin-like complex subunit 5; This family includes HAUS augmin-like complex subunit 5. The HAUS augmin-like complex contributes to mitotic spindle assembly, maintenance of chromosome integrity and completion of cytokinesis.


Pssm-ID: 464332 [Multi-domain]  Cd Length: 643  Bit Score: 41.57  E-value: 2.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  268 QQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQeyaqqmAEMQRAQKEmewqREIARQKAEMDEKEKQRQ 347
Cdd:pfam14817  69 AESRQSAAARRLELQKEIERLRAEISRLDKQLEARELELSREE------AERERALDE----ISDSRHRQLLLEAYDQQC 138
                          90       100       110
                  ....*....|....*....|....*....|
gi 597837628  348 VEIARQMAERQRQEEELLRQQEVALQEAER 377
Cdd:pfam14817 139 EEARKILAEDHQRLQGQLQQLRDAARKAEK 168
Pinin_SDK_memA pfam04696
pinin/SDK/memA/ protein conserved region; Members of this family have very varied ...
373-423 2.65e-03

pinin/SDK/memA/ protein conserved region; Members of this family have very varied localizations within the eukaryotic cell. pinin is known to localize at the desmosomes and is implicated in anchoring intermediate filaments to the desmosomal plaque. SDK2/3 is a dynamically localized nuclear protein thought to be involved in modulation of alternative pre-mRNA splicing. memA is a tumour marker preferentially expressed in human melanoma cell lines. A common feature of the members of this family is that they may all participate in regulating protein-protein interactions.


Pssm-ID: 461396 [Multi-domain]  Cd Length: 130  Bit Score: 38.81  E-value: 2.65e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 597837628  373 QEAERQKKERERQKEIARQVVERKKQEEVRRIEKARKKSEMEKKERERQQE 423
Cdd:pfam04696  23 KEESKQKEKEERRAEIEKRLEEKAKQEKEELEERKREEREELFEERRAEQI 73
FliH COG1317
Flagellar biosynthesis/type III secretory pathway protein FliH [Cell motility, Intracellular ...
284-380 2.86e-03

Flagellar biosynthesis/type III secretory pathway protein FliH [Cell motility, Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 440928 [Multi-domain]  Cd Length: 172  Bit Score: 39.52  E-value: 2.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 284 EELEWQQEIARQEAERQRKEEEMRRQQEYAQQmaEMQRAQKEME-WQREIARQKAEMDEKEKQRQVEIARQMAER----- 357
Cdd:COG1317    2 EELEALREEAREEGYAEGYEEGLEEGRAEAEA--EIAEALEQLQaLLEQLQAPLEELDEELEEELVELALAIARKvigre 79
                         90       100
                 ....*....|....*....|....
gi 597837628 358 -QRQEEELLRQQEVALQEAERQKK 380
Cdd:COG1317   80 lALDPEAILALVREALAALREAEE 103
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
345-529 2.94e-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: 41.50  E-value: 2.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   345 QRQVEIARQMAERQRQEEE------LLRQQEVALQEAERQKKERERQKEIARQVVERKKQEEVRRiEKARKKSEMEKKER 418
Cdd:pfam02463  141 GGKIEIIAMMKPERRLEIEeeaagsRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQ-AKKALEYYQLKEKL 219
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   419 ERQQEIARQHAERQRKEEEARRQEEARLfAERQKKERERQEEIARQMEEEEKRQREeaeKEEMRKRKIEEERLRKEEEQR 498
Cdd:pfam02463  220 ELEEEYLLYLDYLKLNEERIDLLQELLR-DEQEEIESSKQEIEKEEEKLAQVLKEN---KEEEKEKKLQEEELKLLAKEE 295
                          170       180       190
                   ....*....|....*....|....*....|.
gi 597837628   499 IEAQRKAEEERRIEEQLAAREVENQSTVVNP 529
Cdd:pfam02463  296 EELKSELLKLERRKVDDEEKLKESEKEKKKA 326
PRK13709 PRK13709
conjugal transfer nickase/helicase TraI; Provisional
275-408 3.00e-03

conjugal transfer nickase/helicase TraI; Provisional


Pssm-ID: 237478 [Multi-domain]  Cd Length: 1747  Bit Score: 41.32  E-value: 3.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  275 VAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQMAEmqraqkemewqreiaRQKAEMDEKEKQRQVEIARQM 354
Cdd:PRK13709 1627 NSVQPGAGNGEPVTAEVLAQRQAEEAIRRETERRADEIVRKMAE---------------NKPDLPDGKTEQAVRDIAGQE 1691
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 597837628  355 AERQRQEEELLRQQEVALQEaerQKKERERQKEIARQVVERKK-----QEEVRRIEKAR 408
Cdd:PRK13709 1692 RDRAAISEREAALPESVLRE---PQREREAVREVARENLLRERlqqmeRDMVRDLQKEK 1747
PRK09039 PRK09039
peptidoglycan -binding protein;
269-389 3.03e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 40.72  E-value: 3.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 269 QEIARQVAERQQKEREELEWQ-QEIARQEA-ERQRKEEemrRQQEYAQQMAEMQRAQKEME----WQREIARQKAEMDEK 342
Cdd:PRK09039  41 QFFLSREISGKDSALDRLNSQiAELADLLSlERQGNQD---LQDSVANLRASLSAAEAERSrlqaLLAELAGAGAAAEGR 117
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 343 --EKQRQVEIARQMAERQRQEEELLRQQ-----------EVALQEAErqKKERERQKEIA 389
Cdd:PRK09039 118 agELAQELDSEKQVSARALAQVELLNQQiaalrrqlaalEAALDASE--KRDRESQAKIA 175
PRK07353 PRK07353
F0F1 ATP synthase subunit B'; Validated
265-357 3.22e-03

F0F1 ATP synthase subunit B'; Validated


Pssm-ID: 235999 [Multi-domain]  Cd Length: 140  Bit Score: 38.83  E-value: 3.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 265 RQRQQEIARQVAERQQKEREeLEWQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQR---AQKEmEWQREIARQKAEMDE 341
Cdd:PRK07353  42 RTNRAEAKERLAEAEKLEAQ-YEQQLASARKQAQAVIAEAEAEADKLAAEALAEAQAeaqASKE-KARREIEQQKQAALA 119
                         90
                 ....*....|....*.
gi 597837628 342 KEKQRQVEIARQMAER 357
Cdd:PRK07353 120 QLEQQVDALSRQILEK 135
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
257-332 3.29e-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: 3.29e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 597837628   257 NAEMEQLERQRQQEIARQVAErQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQR--AQKEMEWQREI 332
Cdd:smart00935  20 QKQLEKEFKKRQAELEKLEKE-LQKLKEKLQKDAATLSEAAREKKEKELQKKVQEFQRKQQKLQQdlQKRQQEELQKI 96
mukB PRK04863
chromosome partition protein MukB;
262-422 3.36e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 41.48  E-value: 3.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  262 QLERQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQ--MAEMQRAQKEMEWQREIARQKAEM 339
Cdd:PRK04863  488 EVSRSEAWDVARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEfcKRLGKNLDDEDELEQLQEELEARL 567
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  340 DEKEKQrqVEIARQMAERQRQEEELLRQQE----------VALQEAERQKKE--------RERQKEIARQVVERKKQEEV 401
Cdd:PRK04863  568 ESLSES--VSEARERRMALRQQLEQLQARIqrlaarapawLAAQDALARLREqsgeefedSQDVTEYMQQLLERERELTV 645
                         170       180
                  ....*....|....*....|.
gi 597837628  402 RRIEKARKKSEMEKKERERQQ 422
Cdd:PRK04863  646 ERDELAARKQALDEEIERLSQ 666
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
200-523 3.61e-03

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 41.11  E-value: 3.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   200 EFLKQLVRIVEaHQVAINKIEEQVGE--------ERRRGGVEDHEHPAGSFRKQGPSGNFEEGSSNAEMEQLERQRQQEI 271
Cdd:TIGR00618  287 NRARKAAPLAA-HIKAVTQIEQQAQRihtelqskMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVAT 365
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   272 ARQVAERQQKEREE--LEWQQEI-ARQEAERQRKEEEMRRQQEYAQQMAEMQR----------AQKEMEWQREIARQKAE 338
Cdd:TIGR00618  366 SIREISCQQHTLTQhiHTLQQQKtTLTQKLQSLCKELDILQREQATIDTRTSAfrdlqgqlahAKKQQELQQRYAELCAA 445
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   339 MDEKEKQRQVE---IARQMAERQRQEEELLRQQEV-ALQEAERQKKERERQKEIARQVVERKKQEevRRIEKARKKSEME 414
Cdd:TIGR00618  446 AITCTAQCEKLekiHLQESAQSLKEREQQLQTKEQiHLQETRKKAVVLARLLELQEEPCPLCGSC--IHPNPARQDIDNP 523
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   415 KKERERQQEIARQHAERQRKEEEARRQEEARLfaeRQKKERERQEEIARQmEEEEKRQREEAEKEEMRKRKIEEERLRKE 494
Cdd:TIGR00618  524 GPLTRRMQRGEQTYAQLETSEEDVYHQLTSER---KQRASLKEQMQEIQQ-SFSILTQCDNRSKEDIPNLQNITVRLQDL 599
                          330       340
                   ....*....|....*....|....*....
gi 597837628   495 EEQRIEAQRKAEEERRIEEQLAAREVENQ 523
Cdd:TIGR00618  600 TEKLSEAEDMLACEQHALLRKLQPEQDLQ 628
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
258-318 3.88e-03

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


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 37.98  E-value: 3.88e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 597837628  258 AEMEQLERQRqqeiARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQMAE 318
Cdd:pfam20492  62 EEKERLEESA----EMEAEEKEQLEAELAEAQEEIARLEEEVERKEEEARRLQEELEEARE 118
Activator_LAG-3 pfam11498
Transcriptional activator LAG-3; The C.elegans Notch pathway, involved in the control of ...
296-432 4.04e-03

Transcriptional activator LAG-3; The C.elegans Notch pathway, involved in the control of growth, differentiation and patterning in animal development, relies on either of the receptors GLP-1 or LIN-12. Both these receptors promote signalling by the recruitment of LAG-3 to target promoters, where it then acts as a transcriptional activator. LAG-3 works as a ternary complex together with the DNA binding protein, LAG-1. Its N-terminal region adopts an elongated kinked helix that is required for complex assembly.


Pssm-ID: 151935 [Multi-domain]  Cd Length: 476  Bit Score: 40.72  E-value: 4.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  296 EAERQRKEEEMRRQQEYAQQMAEMQRAQKEMewqREIARQKAEMDEKEKQRQVEIARQMAERQRQEEE-----LLRQQEV 370
Cdd:pfam11498 302 EAGGDRMPQSAPPPAMNPQHIAQLAQQQNKM---RLLQQQEMEMQRIEQQRQQQIMHQHQQQQQQEHQqqqmlLQQQQQM 378
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 597837628  371 -ALQEAERQKKERERQKEIARQVVERKKQEEVRRIEKARKKSEMEKKERERQQEIARQHAERQ 432
Cdd:pfam11498 379 hQLQQHHQMNGGGQFATQAHQHAAYLQQMQHMRLQEQIQHQQQQAQHHQQAQQQHQQPAQHGQ 441
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
294-528 4.37e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.81  E-value: 4.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   294 RQEAERQ--RKEEEMRRQQEYAqqmAEMQRAQKEMEWQREIARQKAEMdeKEKQRQVEIARQMAERQRQEEELlRQQEVA 371
Cdd:TIGR02168  174 RKETERKleRTRENLDRLEDIL---NELERQLKSLERQAEKAERYKEL--KAELRELELALLVLRLEELREEL-EELQEE 247
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   372 LQEAERQKKERERQKeiarqvveRKKQEEVRRIEKARkkSEMEKKERERQQEIARQHAERQRKEEEARRQEEARLFAERQ 451
Cdd:TIGR02168  248 LKEAEEELEELTAEL--------QELEEKLEELRLEV--SELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQ 317
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 597837628   452 KKERERQEEIARQMeeeekrqreeaeKEEMRKRKIEEERLRKEEEQRIEAQRKAEEERRIEEQLAAREVENQSTVVN 528
Cdd:TIGR02168  318 LEELEAQLEELESK------------LDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLE 382
flagell_FliJ TIGR02473
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ...
299-464 4.47e-03

flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly every case, in the midst of other flagellar biosynthesis genes in bacgterial genomes. Typically the fliJ gene is found adjacent to the gene for the flagellum-specific ATPase FliI. Sequence scoring in the gray zone between trusted and noise cutoffs include both probable FliJ proteins and components of bacterial type III secretion systems.


Pssm-ID: 131526 [Multi-domain]  Cd Length: 141  Bit Score: 38.45  E-value: 4.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  299 RQRKEEEMRRQQEYAQQMAEMQRAQKEMEwQREIARQKAEMDEKEKQRQVEIARQMAERQRQEEELLRQQEVALQEAERQ 378
Cdd:TIGR02473   9 DLREKEEEQAKLELAKAQAEFERLETQLQ-QLIKYREEYEQQALEKVGAGTSALELSNYQRFIRQLDQRIQQQQQELALL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  379 KKERERQKEIARQvverkKQEEVRRIEKARkksemEKKERERQqeiarqhaerqrkeeearrqeearlfAERQKKERERQ 458
Cdd:TIGR02473  88 QQEVEAKRERLLE-----ARRELKALEKLK-----EKKQKEYR--------------------------AEEAKREQKEM 131

                  ....*.
gi 597837628  459 EEIARQ 464
Cdd:TIGR02473 132 DELATQ 137
DUF1387 pfam07139
Protein of unknown function (DUF1387); This family represents a conserved region approximately ...
236-414 4.62e-03

Protein of unknown function (DUF1387); This family represents a conserved region approximately 300 residues long within a number of hypothetical proteins of unknown function that seem to be restricted to mammals.


Pssm-ID: 462100  Cd Length: 311  Bit Score: 40.11  E-value: 4.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  236 EHPAGSFRKQGPSGNFEEGSSnAEMEQLERQRQQEIARQVAERQQKEREELewQQEIARQEAERQRKEEEM----RRQQe 311
Cdd:pfam07139 122 LSRNASKPKSRPSSNKSLLED-APLSSTDDKLGSSIEKKVGPNIEKSVKDL--QRCTVSLTRYRVVIKEEMdasiKKIK- 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  312 yaQQMAEMQRAQKEMEwqreiARQKAEMDeKEKQRQVEIarqMAERQRQEEELLRQQEVALQEAERQKKE-RERQKEIar 390
Cdd:pfam07139 198 --ATFAELQSCLMDRE-----VALLAEMD-KVKAEAMEI---LTARQKKAEELKRLTDLAVQMSEEQLVElRADIKHF-- 264
                         170       180
                  ....*....|....*....|....
gi 597837628  391 qVVERKKQEEVRRIekARKKSEME 414
Cdd:pfam07139 265 -VSERKYDEELGRA--ARFTCDLE 285
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
233-513 4.82e-03

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 40.72  E-value: 4.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   233 EDHEHPAGSFRKQGPSGNFEEGSSNAEMEQLERQRQQ--EIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQ 310
Cdd:TIGR00618  545 EDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRskEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPE 624
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   311 EYAQQMAEMQRaQKEMEWQREIARQKAEMDEKEKQRQVEIARQMAErqrQEEELLRQQEVALQEAERQKKERERQKEIAR 390
Cdd:TIGR00618  625 QDLQDVRLHLQ-QCSQELALKLTALHALQLTLTQERVREHALSIRV---LPKELLASRQLALQKMQSEKEQLTYWKEMLA 700
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   391 QVVERKKQEEVRRIEKARKKSEMEKKERERQQEIARQHAERQRKEEEARRQEEARLFAERQKKERERQE----------- 459
Cdd:TIGR00618  701 QCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEvtaalqtgael 780
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 597837628   460 -----EIARQMEEEEKRQREEAEKEEMRKRKIEEERLRKEEEQRIEAQRKAEEERRIEE 513
Cdd:TIGR00618  781 shlaaEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEE 839
PKK pfam12474
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino ...
334-432 5.00e-03

Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino acids in length. The family is found in association with pfam00069. Polo-like kinase 1 (Plx1) is essential during mitosis for the activation of Cdc25C, for spindle assembly, and for cyclin B degradation. This family is Polo kinase kinase (PKK) which phosphorylates Polo kinase and Polo-like kinase to activate them. PKK is a serine/threonine kinase.


Pssm-ID: 463600 [Multi-domain]  Cd Length: 139  Bit Score: 38.31  E-value: 5.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  334 RQKAEMDEKEKQRQVEIARQMAERQRQEEELLRQQEVAL-QEAERQKKERERqkeiarqvvERKKQEEVRRIEKARKKSE 412
Cdd:pfam12474  11 RFEQERQQLKKRYEKELEQLERQQKQQIEKLEQRQTQELrRLPKRIRAEQKK---------RLKMFRESLKQEKKELKQE 81
                          90       100
                  ....*....|....*....|
gi 597837628  413 MEKKERERQQEIARQHAERQ 432
Cdd:pfam12474  82 VEKLPKFQRKEAKRQRKEEL 101
HflC COG0330
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ...
268-355 5.18e-03

Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440099 [Multi-domain]  Cd Length: 279  Bit Score: 39.82  E-value: 5.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 268 QQEIARQVAERQQKEREELEWQ----QEIARQEAERQRKEEEMRrqqeyAQQMAEMQRAQKEMEWQREIARQKAEMDEKE 343
Cdd:COG0330  170 QDAMEDRMKAEREREAAILEAEgyreAAIIRAEGEAQRAIIEAE-----AYREAQILRAEGEAEAFRIVAEAYSAAPFVL 244
                         90
                 ....*....|..
gi 597837628 344 KQRQVEIARQMA 355
Cdd:COG0330  245 FYRSLEALEEVL 256
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
374-464 5.62e-03

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 40.49  E-value: 5.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  374 EAERQKKERERQKEIARQVVERKKQEEVRRIEKAR-KKSEMEKKERERqqeIARQHAERQRkeeearrqeearlfAERQK 452
Cdd:PTZ00266  436 ERARIEKENAHRKALEMKILEKKRIERLEREERERlERERMERIERER---LERERLERER--------------LERDR 498
                          90
                  ....*....|..
gi 597837628  453 KERERQEEIARQ 464
Cdd:PTZ00266  499 LERDRLDRLERE 510
Caldesmon pfam02029
Caldesmon;
215-435 5.69e-03

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 40.24  E-value: 5.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  215 AINKIEEQVGEERRRGGVEDHEHPAGSFRKQGPSGNFEEGSSNAEMEQLERQRQQEIARQVAERQQKEREELEWQQEIAR 294
Cdd:pfam02029  92 TIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEVPT 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  295 Q-------EAERQRKEEEM------------RRQQEYAQQMAEMQRAQKEMEWQREIARQKAEMDEKEKQRQVEiARQMA 355
Cdd:pfam02029 172 EnfakeevKDEKIKKEKKVkyeskvfldqkrGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLE-AEQKL 250
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  356 ERQRQeeellRQQEVALQEAERQkkeRERQKEIARQVVERKKQEEVRRieKARkksemEKKERERQQEiarqHAERQRKE 435
Cdd:pfam02029 251 EELRR-----RRQEKESEEFEKL---RQKQQEAELELEELKKKREERR--KLL-----EEEEQRRKQE----EAERKLRE 311
MAT1 pfam06391
CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for ...
336-423 5.80e-03

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


Pssm-ID: 461894 [Multi-domain]  Cd Length: 202  Bit Score: 39.15  E-value: 5.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  336 KAEMDEKEKQRQVEIARQMAERQRQEEELLRQqevalQEAERQKKERERQKEIARQVVERKKQEEVRR------------ 403
Cdd:pfam06391  67 EKKIEQYEKENKDLILKNKMKLSQEEEELEEL-----LELEKREKEERRKEEKQEEEEEKEKKEKAKQelidelmtsnkd 141
                          90       100
                  ....*....|....*....|....
gi 597837628  404 ----IEKARKKSEMEKKERERQQE 423
Cdd:pfam06391 142 aeeiIAQHKKTAKKRKSERRRKLE 165
CAF-1_p150 pfam11600
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ...
320-438 5.97e-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: 38.52  E-value: 5.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  320 QRAQKEMEWQREIARQKAEMDEKEKQRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEiarqvVERKKQE 399
Cdd:pfam11600   1 RRSQKSVQSQEEKEKQRLEKDKERLRRQLKLEAEKEEKERLKEEAKAEKERAKEEARRKKEEEKELKE-----KERREKK 75
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 597837628  400 EVRRIEKARKKSEMEKKERERQQEIARQHAERQRKEEEA 438
Cdd:pfam11600  76 EKDEKEKAEKLRLKEEKRKEKQEALEAKLEEKRKKEEEK 114
NtpE COG1390
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal ...
319-415 6.25e-03

Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 is part of the Pathway/BioSystem: A/V-type ATP synthase


Pssm-ID: 441000 [Multi-domain]  Cd Length: 196  Bit Score: 38.77  E-value: 6.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 319 MQRAQKEMEWQREIARQKAE--MDEKEKQRQvEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVERK 396
Cdd:COG1390   12 LEEAEAEAEEILEEAEEEAEkiLEEAEEEAE-EIKEEILEKAEREAEREKRRIISSAELEARKELLEAKEELIEEVFEEA 90
                         90
                 ....*....|....*....
gi 597837628 397 KQeevrRIEKARKKSEMEK 415
Cdd:COG1390   91 LE----KLKNLPKDPEYKE 105
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
252-463 6.29e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 40.54  E-value: 6.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   252 EEGSSNAEMEQLERQRQQEIARQVAERQQKER----------EELEWQQEI--------ARQEAERQ-----------RK 302
Cdd:pfam01576    5 EEMQAKEEELQKVKERQQKAESELKELEKKHQqlceeknalqEQLQAETELcaeaeemrARLAARKQeleeilhelesRL 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   303 EEEMRRQQEYAQQMAEMQRAQKEMEWQ---REIARQKAEM-----DEKEKQRQVEI-------ARQMAERQRQEEELLRQ 367
Cdd:pfam01576   85 EEEEERSQQLQNEKKKMQQHIQDLEEQldeEEAARQKLQLekvttEAKIKKLEEDIllledqnSKLSKERKLLEERISEF 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   368 QEVALQEAERQK---KERERQKEIARQVVERKKQEEVRRIEKARKKSEMEKKERERQQEIARQHAErqrkeeearrqeEA 444
Cdd:pfam01576  165 TSNLAEEEEKAKslsKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQ------------IA 232
                          250
                   ....*....|....*....
gi 597837628   445 RLFAERQKKERERQEEIAR 463
Cdd:pfam01576  233 ELRAQLAKKEEELQAALAR 251
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
390-519 6.31e-03

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 39.86  E-value: 6.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 390 RQVVERKKQEEVRRIEkARKKSEMEKKERERQQEIARQHAERQRKEEEArrqeearlfAERQKKERERQEEIARQmeeee 469
Cdd:COG2268  192 RKIAEIIRDARIAEAE-AERETEIAIAQANREAEEAELEQEREIETARI---------AEAEAELAKKKAEERRE----- 256
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 597837628 470 krqREE---------AEKEEMRKRKIEEERLRKEEEQRIEAQRKaEEERRIEEQLAARE 519
Cdd:COG2268  257 ---AETaraeaeaayEIAEANAEREVQRQLEIAEREREIELQEK-EAEREEAELEADVR 311
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
295-432 6.53e-03

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


Pssm-ID: 405931 [Multi-domain]  Cd Length: 151  Bit Score: 38.11  E-value: 6.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  295 QEAERQRKEEEMRRQQEyaqqMAEMQRAQKEMEwqreiaRQKAEMdEKEKQRQVEIARQMAERQRqEEELLRQQEVAL-- 372
Cdd:pfam15346   1 KEAESKLLEEETARRVE----EAVAKRVEEELE------KRKDEI-EAEVERRVEEARKIMEKQV-LEELEREREAELee 68
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  373 ----QEAERQKKE------RERQKEIARQvveRKKQEEVRRIEKARKKSEMEKKERERQQEIARQHAERQ 432
Cdd:pfam15346  69 errkEEEERKKREelerilEENNRKIEEA---QRKEAEERLAMLEEQRRMKEERQRREKEEEEREKREQQ 135
SPFH_like_u3 cd03406
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ...
257-327 6.64e-03

Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and, in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.


Pssm-ID: 259804 [Multi-domain]  Cd Length: 293  Bit Score: 39.59  E-value: 6.64e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 597837628 257 NAEMEQLERQRQQEIARQVAerqqkereELEWQQEIARQEAERQRK--EEEMRRQQEYAQQMAEMQRAQKEME 327
Cdd:cd03406  191 EAETERKRAVIEAEKDAEVA--------KIQMQQKIMEKEAEKKISeiEDEMHLAREKARADAEYYRALREAE 255
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
287-397 6.79e-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: 37.95  E-value: 6.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   287 EWQQEIARQEAERQRKEEEMRRQQEYAQQMAEmqraqkemewqrEIARQKAEMDEKEKQ-RQVEIARQMAERQRQEEELl 365
Cdd:smart00935  15 AGKAAQKQLEKEFKKRQAELEKLEKELQKLKE------------KLQKDAATLSEAAREkKEKELQKKVQEFQRKQQKL- 81
                           90       100       110
                   ....*....|....*....|....*....|..
gi 597837628   366 rQQEVALQEAERQKKERERQKEIARQVVERKK 397
Cdd:smart00935  82 -QQDLQKRQQEELQKILDKINKAIKEVAKKKG 112
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
329-404 7.38e-03

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 40.32  E-value: 7.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  329 QREIARQKAEMDE--KEKQRQVEIARQMAERQRQEEELLRQQEVALQEAERQ------------KKERERQKEIARQVVE 394
Cdd:PRK11448  148 QQEVLTLKQQLELqaREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQleqlqekaaetsQERKQKRKEITDQAAK 227
                          90
                  ....*....|..
gi 597837628  395 RKK--QEEVRRI 404
Cdd:PRK11448  228 RLElsEEETRIL 239
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
342-431 8.53e-03

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 39.93  E-value: 8.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  342 KEKQRQVEIARQMAERQRQE-EELLRQQEVALQEAERQKKERERQKEIArQVVERKKQEEVRRIEKARKKSEM-EKKERE 419
Cdd:PRK11448  138 EDPENLLHALQQEVLTLKQQlELQAREKAQSQALAEAQQQELVALEGLA-AELEEKQQELEAQLEQLQEKAAEtSQERKQ 216
                          90
                  ....*....|..
gi 597837628  420 RQQEIARQHAER 431
Cdd:PRK11448  217 KRKEITDQAAKR 228
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
252-526 8.66e-03

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


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 39.82  E-value: 8.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   252 EEGSSNAEMEQLERQrqqEIARQVAERQ-----QKEREELE-WQQEIARQEA-------------ERQRKEEEMRRQQEY 312
Cdd:pfam12128  207 EDDGVVPPKSRLNRQ---QVEHWIRDIQaiagiMKIRPEFTkLQQEFNTLESaelrlshlhfgykSDETLIASRQEERQE 283
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   313 AQQMAEMQRAQKEMEWQREIARQKAEM-----DEKEKQRQVEIARQMAER----------QRQEEELLRQQEVALQEaER 377
Cdd:pfam12128  284 TSAELNQLLRTLDDQWKEKRDELNGELsaadaAVAKDRSELEALEDQHGAfldadietaaADQEQLPSWQSELENLE-ER 362
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   378 QKKERERQKEIARQVVERK---KQEEVRRIEKARKKSEMEKKERERQQEIARQHAERQRKEEEARRQEEARLFAERQKKE 454
Cdd:pfam12128  363 LKALTGKHQDVTAKYNRRRskiKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRL 442
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 597837628   455 RERQEEIARQMEEEEKRQREeaeKEEMRKRKIEEERLRKEEEqrieaQRKAEEERRIEEQLAAREVENQSTV 526
Cdd:pfam12128  443 KSRLGELKLRLNQATATPEL---LLQLENFDERIERAREEQE-----AANAEVERLQSELRQARKRRDQASE 506
PilO COG3167
Type IV pilus assembly protein PilO [Cell motility, Extracellular structures];
279-341 8.67e-03

Type IV pilus assembly protein PilO [Cell motility, Extracellular structures];


Pssm-ID: 442400 [Multi-domain]  Cd Length: 202  Bit Score: 38.39  E-value: 8.67e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 597837628 279 QQKEREELewQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEwqreiaRQ---KAEMDE 341
Cdd:COG3167   44 QLEELEEL--EAEEAQLKQELEKKQAKAANLPALKAQLEELEQQLGELL------KQlpsKAEVPA 101
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
343-414 8.71e-03

ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 39.66  E-value: 8.71e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 597837628 343 EKQRQVEIARQMAERQRQEEELLRQQEVAlqeaeRQKKERERQkeiARQVVERKKQ-EEVRRIEKARKKSEME 414
Cdd:COG0488  238 LEQRAERLEQEAAAYAKQQKKIAKEEEFI-----RRFRAKARK---AKQAQSRIKAlEKLEREEPPRRDKTVE 302
CCDC34 pfam13904
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ...
356-464 8.84e-03

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


Pssm-ID: 464032 [Multi-domain]  Cd Length: 221  Bit Score: 38.53  E-value: 8.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  356 ERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVERKKQEEVRRIEKARKKSE------MEKKERERQQEIARQHA 429
Cdd:pfam13904  65 QRQRQKELQAQKEEREKEEQEAELRKRLAKEKYQEWLQRKARQQTKKREESHKQKAAesasksLAKPERKVSQEEAKEVL 144
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 597837628  430 ERQRKEEEARrqeearlfaERQKKERERQEEIARQ 464
Cdd:pfam13904 145 QEWERKKLEQ---------QQRKREEEQREQLKKE 170
FAM184 pfam15665
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
260-384 8.87e-03

Family with sequence similarity 184, A and B; The function of FAM184 is not known.


Pssm-ID: 464788 [Multi-domain]  Cd Length: 211  Bit Score: 38.49  E-value: 8.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  260 MEQLERQRQQEIARQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKEMEWQREIARQKA-- 337
Cdd:pfam15665  62 LEQHERMKRQALTEFEQYKRRVEERELKAEAEHRQRVVELSREVEEAKRAFEEKLESFEQLQAQFEQEKRKALEELRAkh 141
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 597837628  338 --EMDEKEKQRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERER 384
Cdd:pfam15665 142 rqEIQELLTTQRAQSASSLAEQEKLEELHKAELESLRKEVEDLRKEKKK 190
ATP-synt_B pfam00430
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is ...
266-358 9.04e-03

ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is thought to translocate protons through membrane (inner membrane in mitochondria, thylakoid membrane in plants, cytoplasmic membrane in bacteria). The B subunits are thought to interact with the stalk of the CF(1) subunits. This domain should not be confused with the ab CF(1) proteins (in the head of the ATP synthase) which are found in pfam00006


Pssm-ID: 425677 [Multi-domain]  Cd Length: 132  Bit Score: 37.29  E-value: 9.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  266 QRQQEIARQV--AERQQKEREELEWQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQ-RAQKEMEWQREIARQKAEMDEK 342
Cdd:pfam00430  30 KRRELIADEIaeAEERRKDAAAALAEAEQQLKEARAEAQEIIENAKKRAEKLKEEIVaAAEAEAERIIEQAAAEIEQEKD 109
                          90       100
                  ....*....|....*....|.
gi 597837628  343 E-----KQRQVEIARQMAERQ 358
Cdd:pfam00430 110 RalaelRQQVVALAVQIAEKL 130
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
346-429 9.11e-03

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 39.92  E-value: 9.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 346 RQVEIARQMAERQRQEEELLRQQEVALQeaeRQKKERERQ--KEIArqvvERKKQEEVRRIEKARKKSEMekKERER-QQ 422
Cdd:PRK11091  78 EQLEESRQRLSRLVAKLEEMRERDLELN---VQLKDNIAQlnQEIA----EREKAEEARQEAFEQLKNEI--KEREEtQI 148

                 ....*..
gi 597837628 423 EIARQHA 429
Cdd:PRK11091 149 ELEQQSS 155
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
259-517 9.19e-03

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


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 39.82  E-value: 9.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   259 EMEQLERQRQQEI-ARQVAERQQKEREELEWQQEIAR-------QEAERQRKEEEMRRQQE----YAQQMAEMQRAQKEM 326
Cdd:pfam12128  269 SDETLIASRQEERqETSAELNQLLRTLDDQWKEKRDElngelsaADAAVAKDRSELEALEDqhgaFLDADIETAAADQEQ 348
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   327 E--WQREIARQKAEMD-EKEKQRQVEIARQmAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVErkKQEEVRR 403
Cdd:pfam12128  349 LpsWQSELENLEERLKaLTGKHQDVTAKYN-RRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQ--ALESELR 425
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628   404 IEKARKKSEMEKKERERQQEIARQHAERQRKEEEARRQEEARLFAERQKKERERQEEiarqmeEEEKRQREEAEKEEMRK 483
Cdd:pfam12128  426 EQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDERIERAREEQEA------ANAEVERLQSELRQARK 499
                          250       260       270
                   ....*....|....*....|....*....|....
gi 597837628   484 RKIEEERLRKEEEQRIEAQRKAEEErrIEEQLAA 517
Cdd:pfam12128  500 RRDQASEALRQASRRLEERQSALDE--LELQLFP 531
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
257-485 9.41e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 39.12  E-value: 9.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 257 NAEMEQLERQRQQEIA--RQVAERQQKEREEL-EWQQEIARQEAERQRKEEEMR--RQQ--EYAQQMAEMQRAQKEM-EW 328
Cdd:COG1340   35 NEELKELAEKRDELNAqvKELREEAQELREKRdELNEKVKELKEERDELNEKLNelREEldELRKELAELNKAGGSIdKL 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 329 QREIAR-----QKAEMD-EKEKQRQVEIAR--QMAERQRQEEELLRQQEVALQEAERQKKE----RERQKEIARQVVERK 396
Cdd:COG1340  115 RKEIERlewrqQTEVLSpEEEKELVEKIKEleKELEKAKKALEKNEKLKELRAELKELRKEaeeiHKKIKELAEEAQELH 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 397 KQ--EEVRRIEKARKKSEMEKKE-RERQQEIARQHAErqrkeeearrqeearlFAERQKKERERQEEIARqMEEEEKRQR 473
Cdd:COG1340  195 EEmiELYKEADELRKEADELHKEiVEAQEKADELHEE----------------IIELQKELRELRKELKK-LRKKQRALK 257
                        250
                 ....*....|..
gi 597837628 474 EEAEKEEMRKRK 485
Cdd:COG1340  258 REKEKEELEEKA 269
G_path_suppress pfam15991
G-protein pathway suppressor; This family of proteins inhibits G-protein- and ...
297-389 9.50e-03

G-protein pathway suppressor; This family of proteins inhibits G-protein- and mitogen-activated protein kinase-mediated signal transduction.


Pssm-ID: 464961 [Multi-domain]  Cd Length: 272  Bit Score: 39.13  E-value: 9.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  297 AERQRKEEEMRRQQEyAQQMAEMQRAQKEMEWQREIARQKAEMDEKEKQRQV-------EIAR---QMAERQRQEEELLR 366
Cdd:pfam15991   1 AARPKMSEQMWRALK-RHIMRERERKKQEQEAKMEEERLRREREEREKEDRMtleetkeQILKlekKLADLKEEKHQLFL 79
                          90       100
                  ....*....|....*....|...
gi 597837628  367 QQEVALQEAERQKKERERQKEIA 389
Cdd:pfam15991  80 QLKKVLHEDETRKRQLKEQSELF 102
DUF4515 pfam14988
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ...
261-425 9.76e-03

Domain of unknown function (DUF4515); This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 198 and 469 amino acids in length. There are two completely conserved L residues that may be functionally important.


Pssm-ID: 405647 [Multi-domain]  Cd Length: 206  Bit Score: 38.21  E-value: 9.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  261 EQLERQRQQEIArQVAERQQKEREELEWQQEIARQEAERQRKEEEMRRQQeyAQQMAEMQRAQKEMEW-----QREIARQ 335
Cdd:pfam14988  21 EKLWNQYVQECE-EIERRRQELASRYTQQTAELQTQLLQKEKEQASLKKE--LQALRPFAKLKESQEReiqdlEEEKEKV 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628  336 KAEMDEKEKQRQVEIARQMAERQRQEEEL------------LRQQEVALQEAERQ----------KKERERQKEIARQVv 393
Cdd:pfam14988  98 RAETAEKDREAHLQFLKEKALLEKQLQELrilelgeratreLKRKAQALKLAAKQalsefcrsikRENRQLQKELLQLI- 176
                         170       180       190
                  ....*....|....*....|....*....|..
gi 597837628  394 erkkqEEVRRIEKARKKSEMEKKERERQQEIA 425
Cdd:pfam14988 177 -----QETQALEAIKSKLENRKQRLKEEQWYL 203
PspC_subgroup_1 NF033838
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ...
251-581 9.92e-03

pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.


Pssm-ID: 468201 [Multi-domain]  Cd Length: 684  Bit Score: 39.61  E-value: 9.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 251 FEEGSSNAEMEQLERQRQQEIARQVAERQQKER--------------EELEWQQEIARQEAER-QRKEEEMRRQQEYAQQ 315
Cdd:NF033838 130 FKKDTLEPGKKVAEATKKVEEAEKKAKDQKEEDrrnyptntyktlelEIAESDVEVKKAELELvKEEAKEPRDEEKIKQA 209
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 316 MAEMQRAQKEMEWQREIA--RQKAEMDEKEKQ--RQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQ 391
Cdd:NF033838 210 KAKVESKKAEATRLEKIKtdREKAEEEAKRRAdaKLKEAVEKNVATSEQDKPKRRAKRGVLGEPATPDKKENDAKSSDSS 289
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 392 V-----------VERKKQEEVRRIEKARKKSEMEKKERERQ-QEIARQHAERQRKEEEARRQEEARLFAERQKKERERQE 459
Cdd:NF033838 290 VgeetlpspslkPEKKVAEAEKKVEEAKKKAKDQKEEDRRNyPTNTYKTLELEIAESDVKVKEAELELVKEEAKEPRNEE 369
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 460 EIarqmeEEEKRQREEAEKEEMRKRKIEEERLRKEEeqriEAQRK-AEEERRIEEQLAAREVENQSTVVNPAFGMHIPGE 538
Cdd:NF033838 370 KI-----KQAKAKVESKKAEATRLEKIKTDRKKAEE----EAKRKaAEEDKVKEKPAEQPQPAPAPQPEKPAPKPEKPAE 440
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 597837628 539 TQAGEHSTDYYG---YSTNSDATktvlaglmsmSSRLTSTEPPQLE 581
Cdd:NF033838 441 QPKAEKPADQQAeedYARRSEEE----------YNRLTQQQPPKTE 476
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
257-525 9.97e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.12  E-value: 9.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 257 NAEMEQLERQRQQEIARQVAERQQ-----KEREELewQQEIARQEAERQRKEEEMRRQQEYAQQMAEMQRAQKE--MEWQ 329
Cdd:COG4372   79 EEELEELNEQLQAAQAELAQAQEEleslqEEAEEL--QEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEelKELE 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 330 REIARQKAEMDEKEKQRQVEIARQMAERQRQEEELLRQQEVALQEAERQKKERERQKEIARQVVERKKQEEVRRIEKARK 409
Cdd:COG4372  157 EQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALS 236
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 597837628 410 KSEMEKKERERQQEIARQHAERQRKEEEARRQEEARLFAERQKKERERQEEIARQMEEEEKRQREEAEKEEMRKRKIEEE 489
Cdd:COG4372  237 ALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDA 316
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 597837628 490 RLRKEEEQRIEAQRKAEEERRIEEQLAAREVENQST 525
Cdd:COG4372  317 LLAALLELAKKLELALAILLAELADLLQLLLVGLLD 352
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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