NCBI Conserved Domain Search

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...

117-403

7.75e-14

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.

Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 75.83 E-value: 7.75e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 117 QLEDLIGMIKSAEKNILLLNQARVRALED----LEKILSEKEELQREINGLEMRLAETDTRIEVAAQEKvhvELLEDQFE 192
Cdd:TIGR04523 339 QLNEQISQLKKELTNSESENSEKQRELEEkqneIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLN---QQKDEQIK 415

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 193 ELQKQLNfssgtvqsmngnlndipidSLTKELHLLKSENIVLKNDIQTLKEELSnvknadqhlaflekersVLESSLKDL 272
Cdd:TIGR04523 416 KLQQEKE-------------------LLEKEIERLKETIIKNNSEIKDLTNQDS-----------------VKELIIKNL 459

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 273 ESKLSTSQEdgsKLSDLNAECMDLRNRVEHLQVLLDKATKQADQAIrvlQQNQELQEKVEKLEE--SLEKANVFKLSSEK 350
Cdd:TIGR04523 460 DNTRESLET---QLKVLSRSINKIKQNLEQKQKELKSKEKELKKLN---EEKKELEEKVKDLTKkiSSLKEKIEKLESEK 533

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1731025460 351 LQQENELMQQKIDLLEDRLQSSDEELQSYIKLYQESVKEFQDTLDTIKKASKK 403
Cdd:TIGR04523 534 KEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEE 586

RfaB

COG0438

Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...

856-969

1.23e-12

Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];

Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 65.40 E-value: 1.23e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 856 IYAASDMFIIPSIFEPCGLTQMIAMRYGSIPIVRKTGGLNDSVFDVDdettptelqNGYTFLTPDEQGLNNALERAfshy 935
Cdd:COG0438    17 LLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGE---------TGLLVPPGDPEALAEAILRL---- 83

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1731025460 936 LNNPSSWQQLVQ---KVMDVDFSWETSAAQYEELYSK 969
Cdd:COG0438    84 LEDPELRRRLGEaarERAEERFSWEAIAERLLALYEE 120

SMC_prok_A

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

118-404

2.23e-12

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: 71.25 E-value: 2.23e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  118 LEDLIGMIKSAEKNILLLNQARVRALEDLEKILSEKEELQREINGLEMRLAETDTRI----EVAAQEKVHVELLED---- 189
Cdd:TIGR02169  711 LSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIeeleEDLHKLEEALNDLEArlsh 790

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  190 -QFEELQKQLNFSSGTVQSMNGNLNDipIDSLTKELHL-----------LKSENIVLKN----------DIQTLKEEL-S 246
Cdd:TIGR02169  791 sRIPEIQAELSKLEEEVSRIEARLRE--IEQKLNRLTLekeylekeiqeLQEQRIDLKEqiksiekeieNLNGKKEELeE 868

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  247 NVKNADQHLAFLEKERSVLESSLKDLESKLSTSQEdgsKLSDLNAECMDLRNRVEHLqvlldKATKQAdqairVLQQNQE 326
Cdd:TIGR02169  869 ELEELEAALRDLESRLGDLKKERDELEAQLRELER---KIEELEAQIEKKRKRLSEL-----KAKLEA-----LEEELSE 935

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1731025460  327 LQEKVEKLEESLEKanvfKLSSEKLQQENELMQQKIDLLEDRLQSSDEELQSYIKLYQEsVKEFQDTLDTIKKASKKT 404
Cdd:TIGR02169  936 IEDPKGEDEEIPEE----ELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDE-LKEKRAKLEEERKAILER 1008

Smc

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

130-377

5.17e-12

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.97 E-value: 5.17e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 130 KNILLLNQARvRALEDLEKILSEKEELQREINGLEMRLAETDTRIEVAAQEkvhVELLEDQFEELQKQLNFSSGTvqsmn 209
Cdd:COG1196   226 EAELLLLKLR-ELEAELEELEAELEELEAELEELEAELAELEAELEELRLE---LEELELELEEAQAEEYELLAE----- 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 210 gnlndipIDSLTKELHLLKSENIVLKNDIQTLKEELsnvKNADQHLAFLEKERSVLESSLKDLESKLSTSQEdgsKLSDL 289
Cdd:COG1196   297 -------LARLEQDIARLEERRRELEERLEELEEEL---AELEEELEELEEELEELEEELEEAEEELEEAEA---ELAEA 363

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 290 NAEcmdLRNRVEHLQVLLDKATKQADQAIRVLQQNQELQEKVEKLEESLEKANvfKLSSEKLQQENELMQQKIDLLEDRL 369
Cdd:COG1196   364 EEA---LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL--ERLERLEEELEELEEALAELEEEEE 438


                  ....*...
gi 1731025460 370 QSSDEELQ 377
Cdd:COG1196   439 EEEEALEE 446

SMC_prok_A

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

118-376

7.07e-12

Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 69.71 E-value: 7.07e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  118 LEDLIGMIKSAEKNILLLNQARVRA-----LEDLEKILSEKEELQREINGLEMRLAETDTRIE-------VAAQEKVH-- 183
Cdd:TIGR02169  220 KREYEGYELLKEKEALERQKEAIERqlaslEEELEKLTEEISELEKRLEEIEQLLEELNKKIKdlgeeeqLRVKEKIGel 299

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  184 ---VELLEDQFEELQKQLNFSSGTVQSmngnlndipidsLTKELHLLKSENIVLKNDIQTLKEELSNVKNAdqhLAFLEK 260
Cdd:TIGR02169  300 eaeIASLERSIAEKERELEDAEERLAK------------LEAEIDKLLAEIEELEREIEEERKRRDKLTEE---YAELKE 364

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  261 ERSVLESSLKDLESKLSTSQEDGS----KLSDLNAECMDLRNRVEHLQVLLDKAT-KQAD---QAIRVLQQNQELQEKVE 332
Cdd:TIGR02169  365 ELEDLRAELEEVDKEFAETRDELKdyreKLEKLKREINELKRELDRLQEELQRLSeELADlnaAIAGIEAKINELEEEKE 444

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1731025460  333 KLEESLEKANvFKLSS-----EKLQQENELMQQKIDLLEDRLQSSDEEL 376
Cdd:TIGR02169  445 DKALEIKKQE-WKLEQlaadlSKYEQELYDLKEEYDRVEKELSKLQREL 492

DR0291

COG1579

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

141-340

8.31e-12

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: 66.10 E-value: 8.31e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 141 RALEDLEKILSEKEELQREINGLEMRLAETDTRIEVaaqekvhvelLEDQFEELQKQlnfssgtvqsmngnlndipIDSL 220
Cdd:COG1579     7 RALLDLQELDSELDRLEHRLKELPAELAELEDELAA----------LEARLEAAKTE-------------------LEDL 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 221 TKELHLLKSENIVLKNDIQTLKEELSNVKNAD-----QH-LAFLEKERSVLESSLKDLESKLSTSQEDgskLSDLNAECM 294
Cdd:COG1579    58 EKEIKRLELEIEEVEARIKKYEEQLGNVRNNKeyealQKeIESLKRRISDLEDEILELMERIEELEEE---LAELEAELA 134

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1731025460 295 DLRNRVEHLQVLLDKATKQADQAIrvlqqnQELQEKVEKLEESLEK 340
Cdd:COG1579   135 ELEAELEEKKAELDEELAELEAEL------EELEAEREELAAKIPP 174

PRK03918

DNA double-strand break repair ATPase Rad50;

125-403

9.13e-12

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 69.32 E-value: 9.13e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 125 IKSAEKNILLLNQARV------RALEDLEKiLSEKEELQREINGLEMRLAETDTRIEVAAQEKVHVELLEDQFEELQKQL 198
Cdd:PRK03918  421 IKELKKAIEELKKAKGkcpvcgRELTEEHR-KELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLK 499

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 199 NFSSgTVQSMNGNLNDIPIDSL---TKELHLLKSENIVLKNDIQTLKEELSNVKNADQHLAFLEKERSVLESSLKDLESK 275
Cdd:PRK03918  500 ELAE-QLKELEEKLKKYNLEELekkAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKE 578

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 276 L-----STSQEDGSKLSDLNA---ECMDLRNRVEHLQVLLDKATKQADQAIRVLQQNQELQEKVEKLEESLEKANVfKLS 347
Cdd:PRK03918  579 LeelgfESVEELEERLKELEPfynEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEK-KYS 657

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1731025460 348 SEKLQQENELMQQKIDLLEdRLQSSDEELQSYIKLYQESVKEFQDTLDTIKKASKK 403
Cdd:PRK03918  658 EEEYEELREEYLELSRELA-GLRAELEELEKRREEIKKTLEKLKEELEEREKAKKE 712

SMC_prok_B

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

135-410

1.04e-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: 69.32 E-value: 1.04e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  135 LNQARVRALEDLEKILSEKEELQREINGLEMRLAETDTRIEVaaqekvhvelLEDQFEELQKQLNFSSGTVQSMNGNL-- 212
Cdd:TIGR02168  237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSE----------LEEEIEELQKELYALANEISRLEQQKqi 306

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  213 -------NDIPIDSLTKELHLLKSENIVLKNDIQTLKEELS----NVKNADQHLAFLEKERSVLESSLKDLESKLSTSQE 281
Cdd:TIGR02168  307 lrerlanLERQLEELEAQLEELESKLDELAEELAELEEKLEelkeELESLEAELEELEAELEELESRLEELEEQLETLRS 386

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  282 D----GSKLSDLNAECMDLRNRVEHLQVLLDKATKQADQAIRVLQQNQ--ELQEKVEKLEESLEKA----NVFKLSSEKL 351
Cdd:TIGR02168  387 KvaqlELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAElkELQAELEELEEELEELqeelERLEEALEEL 466

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1731025460  352 QQENELMQQKIDLLEDRLQSSDEELQSYIKLyQESVKEFQDTLDTIKKASKKTATDEPV 410
Cdd:TIGR02168  467 REELEEAEQALDAAERELAQLQARLDSLERL-QENLEGFSEGVKALLKNQSGLSGILGV 524

SMC_prok_B

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

106-390

1.04e-11

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 69.32 E-value: 1.04e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  106 EVDTEGLNKGVQLEDLIGMIKSAEKNILLLNQARVRALEDLEKILSEKEELQREINGLEMRLAETDTRIEVAAQEKvhvE 185
Cdd:TIGR02168  709 ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEI---E 785

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  186 LLEDQFEELQKQLNfssgtvqsmngnLNDIPIDSLTKELHLLKSENIVLKNDIQTLKEELSNVK----NADQHLAFLEKE 261
Cdd:TIGR02168  786 ELEAQIEQLKEELK------------ALREALDELRAELTLLNEEAANLRERLESLERRIAATErrleDLEEQIEELSED 853

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  262 RSVLESSLKDLESKLSTSQEDGSKLSDLNAECMDLRNRVEHLQVLLDKATKQADQAIRVLQQN-QELQEKVEKLEESLEK 340
Cdd:TIGR02168  854 IESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRElEELREKLAQLELRLEG 933

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1731025460  341 ANVfKLSS--EKLQQENELMQQKIDLLEDRLQSSDEELQSYIKLYQESVKEF 390
Cdd:TIGR02168  934 LEV-RIDNlqERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984

GT4_sucrose_synthase

cd03800

sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...

500-964

1.10e-11

sucrose-phosphate synthase and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. The sucrose-phosphate synthases in this family may be unique to plants and photosynthetic bacteria. This enzyme catalyzes the synthesis of sucrose 6-phosphate from fructose 6-phosphate and uridine 5'-diphosphate-glucose, a key regulatory step of sucrose metabolism. The activity of this enzyme is regulated by phosphorylation and moderated by the concentration of various metabolites and light.

Pssm-ID: 340830 [Multi-domain] Cd Length: 398 Bit Score: 68.04 E-value: 1.10e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 500 GGLGDVITGLSKALQSRGHLVEIvlpkydcmeYSRIKDLRLLDVVLESyfdgrlfkNKIWVGTVEGLPVYFIephhPDKF 579
Cdd:cd03800    21 GGQNVYVLELARALAELGYQVDI---------FTRRISPADPEVVEIA--------PGARVIRVPAGPPEYL----PKEE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 580 FWRaqYYGEhddfkrfsyFSRAALELLLRAGKRPDIIHCHdwqtafiaplYWDlyypKGLNSARI--------CFTCHNF 651
Cdd:cd03800    80 LWP--YLEE---------FADGLLRFIAREGGRYDLIHSH----------YWD----SGLVGALLarrlgvplVHTFHSL 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 652 E-----YQGTAPASDlASCGLDVDQ--LNRQDRLqdnssherinpvkgavvfsnIVTTvsptyAQEVRraegghGLHSTL 724
Cdd:cd03800   135 GrvkyrHLGAQDTYH-PSLRITAEEqiLEAADRV--------------------IAST-----PQEAD------ELISLY 182

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 725 NFHSKKFFGILNGIDTDVWNPSTDsfikvqynandlqgkaenKDALRRHLGLSSNvrKPLVGCITRLVPQKGIH-LIR-Y 802
Cdd:cd03800   183 GADPSRINVVPPGVDLERFFPVDR------------------AEARRARLLLPPD--KPVVLALGRLDPRKGIDtLVRaF 242

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 803 AIYRTLELGGQFVL-LGSSPVPHIQREFED--IANHFQSHDQIRLVLAYDESLSHWIYAASDMFIIPSIFEPCGLTQMIA 879
Cdd:cd03800   243 AQLPELRELANLVLvGGPSDDPLSMDREELaeLAEELGLIDRVRFPGRVSRDDLPELYRAADVFVVPSLYEPFGLTAIEA 322

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 880 MRYGsIPIV-RKTGGLNDSVFDvddettpteLQNGytFLTP--DEQGLNNALERAFShylnNPSSWQQL----VQKVMDV 952
Cdd:cd03800   323 MACG-TPVVaTAVGGLQDIVRD---------GRTG--LLVDphDPEALAAALRRLLD----DPALWQRLsragLERARAH 386

                         490
                  ....*....|..
gi 1731025460 953 dFSWETSAAQYE 964
Cdd:cd03800   387 -YTWESVADQLL 397

EnvC

COG4942

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

117-341

1.14e-11

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: 67.48 E-value: 1.14e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 117 QLEDLIGMIKSAEKNILLLNQARVRALEDLEKILSEKEELQREINGLEMRLAETDTRIEVAAQEKVHVEL-LEDQFEELQ 195
Cdd:COG4942    28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAeLEAQKEELA 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 196 KQLN--FSSGTVQSMNGNLNDIPIDSLTKELHLLKSENIVLKNDIQTLKEELSNvknadqhlafLEKERSVLESSLKDLE 273
Cdd:COG4942   108 ELLRalYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE----------LAALRAELEAERAELE 177

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1731025460 274 SKLSTSQEDGSKLSdlnaecmDLRNRVEHLQVLLDKATKQADQAIRVLQQN-QELQEKVEKLEESLEKA 341
Cdd:COG4942   178 ALLAELEEERAALE-------ALKAERQKLLARLEKELAELAAELAELQQEaEELEALIARLEAEAAAA 239

SMC_prok_A

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

140-416

1.21e-11

Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 68.94 E-value: 1.21e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  140 VRALEDLEKILSEKEELQREINGLEMRLAETDTRIEVAAQEkvhVELLEDQFEELQKQLNFSSGTVQSMNGNLNDIP--I 217
Cdd:TIGR02169  670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQE---LSDASRKIGEIEKEIEQLEQEEEKLKERLEELEedL 746

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  218 DSLTKELHLLKSENIVLKNDIQTLKEELSNVKNA----------------DQHLAFLEKERSVLESSLKDLESKLSTSQE 281
Cdd:TIGR02169  747 SSLEQEIENVKSELKELEARIEELEEDLHKLEEAlndlearlshsripeiQAELSKLEEEVSRIEARLREIEQKLNRLTL 826

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  282 DGSKLSDLnaecmdlrnrVEHLQVLLDKATKQADQairVLQQNQELQEKVEKLEESLEK--ANVFKLSSE--KLQQENEL 357
Cdd:TIGR02169  827 EKEYLEKE----------IQELQEQRIDLKEQIKS---IEKEIENLNGKKEELEEELEEleAALRDLESRlgDLKKERDE 893

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1731025460  358 MQQKIDLLEDRLQ---SSDEELQSYIKLYQESVKEFQDTLDTIKKAsKKTATDEPVNDMPWE 416
Cdd:TIGR02169  894 LEAQLRELERKIEeleAQIEKKRKRLSELKAKLEALEEELSEIEDP-KGEDEEIPEEELSLE 954

SMC_prok_B

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

127-400

4.63e-11

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.00 E-value: 4.63e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  127 SAEKNILLLNQARVRALEDLEKILSEKEELQREINGLEMRLAETDTRIEVAAQEKvhvELLEDQFEELQKQLNFSSGTVQ 206
Cdd:TIGR02168  667 KTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKEL---EELSRQISALRKDLARLEAEVE 743

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  207 smngnlndipidSLTKELHLLKSENIVLKNDIQTLKEELSnvkNADQHLAFLEKERSVLESSLKDLESKLSTSQEDGSKL 286
Cdd:TIGR02168  744 ------------QLEERIAQLSKELTELEAEIEELEERLE---EAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL 808

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  287 ----SDLNAECMDLRNRVEHLQvlldkatkqaDQAIRVLQQNQELQEKVEKLEESLEKANvfkLSSEKLQQENELMQQKI 362
Cdd:TIGR02168  809 raelTLLNEEAANLRERLESLE----------RRIAATERRLEDLEEQIEELSEDIESLA---AEIEELEELIEELESEL 875

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1731025460  363 DLLEDRLQSSDEELQSYIKLYQESVKEFQDTLDTIKKA 400
Cdd:TIGR02168  876 EALLNERASLEEALALLRSELEELSEELRELESKRSEL 913

Mplasa_alph_rch

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...

113-402

8.50e-11

Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 66.20 E-value: 8.50e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 113 NKGVQLEDLIGMIKS-AEKNILLLNQarvraLEDLEKILSE----KEELQREINGLEMRLAETDTRIEVAAQEKVHVEll 187
Cdd:TIGR04523 194 NKLLKLELLLSNLKKkIQKNKSLESQ-----ISELKKQNNQlkdnIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIK-- 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 188 eDQFEELQKQLNFSSGTvqsmngnlndipIDSLTKELHLLKSENIVLKND-----IQTLKEELSNVKNadqhlafleker 262
Cdd:TIGR04523 267 -KQLSEKQKELEQNNKK------------IKELEKQLNQLKSEISDLNNQkeqdwNKELKSELKNQEK------------ 321

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 263 svlesSLKDLESKLSTSQEdgsKLSDLNAECMDLRNRVEHLQvlLDKATKQadqairvlqqnQELQEKVEKLEESLEKAN 342
Cdd:TIGR04523 322 -----KLEEIQNQISQNNK---IISQLNEQISQLKKELTNSE--SENSEKQ-----------RELEEKQNEIEKLKKENQ 380

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 343 VFKLSSEKLQQENELMQQKIDLLEDRLQSSDEELQSYIKLYQESVKEFQDTLDTIKKASK 402
Cdd:TIGR04523 381 SYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNS 440

GT4_WcaC-like

cd03825

putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...

611-969

2.73e-10

putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Escherichia coli WcaC has been predicted to function in colanic acid biosynthesis. WcfI in Bacteroides fragilis has been shown to be involved in the capsular polysaccharide biosynthesis.

Pssm-ID: 340851 [Multi-domain] Cd Length: 364 Bit Score: 63.12 E-value: 2.73e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 611 KRPDIIHCHDWQTAF--IAPLYWDLYYPKGLNSARIC--FT--CHNF-------EYQGTAPasdlascgldvdQLNRQDR 677
Cdd:cd03825    50 IEADIIHLHWIHGGYlsLKALFKLLRRKPVVWTLHDMwpFTggCHYPmecegwkTGCGNCP------------NLNSYPP 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 678 LQDNSSHERINPVKGAVVFSNI-VTTVSPTYAQEVRRaegghglhSTLNFHSKKFFgILNGIDTDVWNPStdsfikvqyn 756
Cdd:cd03825   118 AKKDLSRQLFRRKREALAKKRLtIVAPSRWLADMVRR--------SPLLKGLPVVV-IPNGIDTEIFAPV---------- 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 757 andlqgkaeNKDALRRHLGLSSNVRKPLVGCITRLVPQKGIHLIRYAI-----YRTLEL---GGQFVLLGSSPVPHIQRE 828
Cdd:cd03825   179 ---------DKAKARKRLGIPQDKKVILFGAESVTKPRKGFDELIEALkllatKDDLLLvvfGKNDPQIVILPFDIISLG 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 829 FEDianhfqshDQIRLVLaydeslshwIYAASDMFIIPSIFEPCGLTQMIAMRYGSIPIVRKTGGLNDSVFDvddettpt 908
Cdd:cd03825   250 YID--------DDEQLVD---------IYSAADLFVHPSLADNLPNTLLEAMACGTPVVAFDTGGSPEIVQH-------- 304

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1731025460 909 eLQNGYTFLTPDEQGLNNALErafsHYLNNPSSWQQLVQKVMDV---DFSWETSAAQYEELYSK 969
Cdd:cd03825   305 -GVTGYLVPPGDVQALAEAIE----WLLANPKERESLGERARALaenHFDQRVQAQRYLELYKD 363

COG4913

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

154-395

5.76e-10

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

Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.40 E-value: 5.76e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  154 EELQREINGLEMRLAETDTRIEVAAQEKvhvELLEDQFEELQKQLNFSSgtvqsmngnlNDIPIDSLTKElhllkseniv 233
Cdd:COG4913    613 AALEAELAELEEELAEAEERLEALEAEL---DALQERREALQRLAEYSW----------DEIDVASAERE---------- 669

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  234 lkndIQTLKEELSNVKNADQHLAFLEKERSVLESSLKDLEsklstsqedgSKLSDLNAECMDLRNRVEHLQVLLDKATKQ 313
Cdd:COG4913    670 ----IAELEAELERLDASSDDLAALEEQLEELEAELEELE----------EELDELKGEIGRLEKELEQAEEELDELQDR 735

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  314 ADQAIRvlQQNQELQEKVEKLEESLEKANVFKLSSEKLQQENELMQQKIDLLEDRLQssdEELQSYIKLYQESVKEFQDT 393
Cdd:COG4913    736 LEAAED--LARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELE---RAMRAFNREWPAETADLDAD 810


                   ..
gi 1731025460  394 LD 395
Cdd:COG4913    811 LE 812

Tropomyosin_1

pfam12718

Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ...

285-388

6.72e-10

Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.

Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 58.47 E-value: 6.72e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 285 KLSDLNAECMDLRNRVEHLQVLLDKA---TKQADQAIRVLQ-QNQELQEKVEKLEESLEKANVFKLSSEKLQQENELMQQ 360
Cdd:pfam12718   1 KMNSLKLEAENAQERAEELEEKVKELeqeNLEKEQEIKSLThKNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNNENLTR 80

                          90       100
                  ....*....|....*....|....*....
gi 1731025460 361 KIDLLEDRLQSSDEELQSYI-KLYQESVK 388
Cdd:pfam12718  81 KIQLLEEELEESDKRLKETTeKLRETDVK 109

COG4372

Uncharacterized protein, contains DUF3084 domain [Function unknown];

132-445

1.26e-09

Uncharacterized protein, contains DUF3084 domain [Function unknown];

Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 61.46 E-value: 1.26e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 132 ILLLNQARVRALEDLEKILSEKEELQREINGLEMRLAETDTRIEVAAQEkvhVELLEDQFEELQKQLnfssgtvQSMNGN 211
Cdd:COG4372    26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSE---LEQLEEELEELNEQL-------QAAQAE 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 212 LNDipidsLTKELHLLKSENIVLKNDIQTLKEELSNvknadqhlafLEKERSVLESSLKDLESKLSTSQEdgsKLSDLNA 291
Cdd:COG4372    96 LAQ-----AQEELESLQEEAEELQEELEELQKERQD----------LEQQRKQLEAQIAELQSEIAEREE---ELKELEE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 292 ECMDLRNRVEHLQVLLDKATKQ-ADQAIRVLQQNQELQEKVEKLEESLEKANVFKLSSEKLQQENELMQQKIDLLEDRLQ 370
Cdd:COG4372   158 QLESLQEELAALEQELQALSEAeAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSA 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1731025460 371 SSDEELQSYIKLYQESVKEFQDTLDTIKKASKKTATDEPVNDMPWEFWSRLLLLIDGWLLEEKISGDDAKLLKEM 445
Cdd:COG4372   238 LLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGA 312

Smc

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

117-377

1.49e-09

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.26 E-value: 1.49e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 117 QLEDLIGMIKSAEKNILLLNQARVRALEDLEKILSEKEELQREINGLEMRLAETDTRIEVAAQEKvhvELLEDQFEELQK 196
Cdd:COG1196   247 ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR---RELEERLEELEE 323

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 197 QlnfssgtvqsmngnlndipIDSLTKELHLLKSENIVLKNDIQTLKEELsnvKNADQHLAFLEKERSVLESSLKDLESKL 276
Cdd:COG1196   324 E-------------------LAELEEELEELEEELEELEEELEEAEEEL---EEAEAELAEAEEALLEAEAELAEAEEEL 381

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 277 STSQEDgskLSDLNAECMDLRNRVEHLQVLLDKATKQADQAIRVLQQNQELQEKVEKLEESLEKANVfKLSSEKLQQENE 356
Cdd:COG1196   382 EELAEE---LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE-EAAEEEAELEEE 457

                         250       260
                  ....*....|....*....|.
gi 1731025460 357 LMQQKIDLLEDRLQSSDEELQ 377
Cdd:COG1196   458 EEALLELLAELLEEAALLEAA 478

EnvC

COG4942

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

132-377

1.56e-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: 60.93 E-value: 1.56e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 132 ILLLNQARVRALEDLEKILSEKEELQREINGLEMRLAETDTRIEVaaqekvhvelLEDQFEELQKQLNFSSGTVQSMNGN 211
Cdd:COG4942     8 ALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKA----------LLKQLAALERRIAALARRIRALEQE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 212 LNDipidsLTKELHLLKSENIVLKNDIQTLKEELSNVKNADQHLAFLEKERSVLESSlkDLESKLSTSQEDGSKLSDLNA 291
Cdd:COG4942    78 LAA-----LEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPE--DFLDAVRRLQYLKYLAPARRE 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 292 ECMDLRNRVEHLQVLLDKATKQADQAIRVLQQNQELQEKVEKLEESLEKAnVFKLSSEKLQQENEL--MQQKIDLLEDRL 369
Cdd:COG4942   151 QAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKL-LARLEKELAELAAELaeLQQEAEELEALI 229


                  ....*...
gi 1731025460 370 QSSDEELQ 377
Cdd:COG4942   230 ARLEAEAA 237

Myosin_tail_1

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

137-396

2.60e-09

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: 61.34 E-value: 2.60e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  137 QARVRALEDLEKIL-SEKEELQREINGLEMRLAEtdtriEVAAQEKVHVE----------------LLEDQFEELQKQLN 199
Cdd:pfam01576   81 ESRLEEEEERSQQLqNEKKKMQQHIQDLEEQLDE-----EEAARQKLQLEkvtteakikkleedilLLEDQNSKLSKERK 155

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  200 FSSGTVQSMNGNLNDIpiDSLTKELHLLKSENIVLKNDIQT-LKEElsnvknadqhlaflEKERSVLESSLKDLESKLST 278
Cdd:pfam01576  156 LLEERISEFTSNLAEE--EEKAKSLSKLKNKHEAMISDLEErLKKE--------------EKGRQELEKAKRKLEGESTD 219

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  279 SQEdgsKLSDLNAECMDLR----NRVEHLQVLLDKATKQADQAIRVLQQNQELQEKVEKLEESLEkanvfklsSEKlQQE 354
Cdd:pfam01576  220 LQE---QIAELQAQIAELRaqlaKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLE--------SER-AAR 287

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1731025460  355 NELMQQKIDLledrlqssDEELqsyiklyqESVK-EFQDTLDT 396
Cdd:pfam01576  288 NKAEKQRRDL--------GEEL--------EALKtELEDTLDT 314

Smc

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

125-341

3.50e-09

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.11 E-value: 3.50e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 125 IKSAEKNILLLNQARVRALEDLEKILSEKEELQREINGLEMRLAETDTRIEVAAQEKVHVELLEDQFEELQKQLnfssgt 204
Cdd:COG1196   297 LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA------ 370

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 205 VQSMNGNLNDipIDSLTKELHLLKSENIVLKNDIQTLKEELsnvKNADQHLAFLEKERSVLESSLKDLESKLSTSQEdgs 284
Cdd:COG1196   371 EAELAEAEEE--LEELAEELLEALRAAAELAAQLEELEEAE---EALLERLERLEEELEELEEALAELEEEEEEEEE--- 442

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1731025460 285 KLSDLNAECMDLRNRVEHLQVLLDKATKQADQAIRVLQQNQELQEKVEKLEESLEKA 341
Cdd:COG1196   443 ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA 499

Glycosyltransferase_GTB-type

cd01635

glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...

768-900

5.12e-09

glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.

Pssm-ID: 340816 [Multi-domain] Cd Length: 235 Bit Score: 57.80 E-value: 5.12e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 768 DALRRHLGLSSNVRKPLVGC----ITRLVPQKGIH-LIR-YAIYRTLELGGQFVLLGSSPVPhiQREFEDIANHFQSHDQ 841
Cdd:cd01635    92 ESTRSELLALARLLVSLPLAdkvsVGRLVPEKGIDlLLEaLALLKARLPDLVLVLVGGGGER--EEEEALAAALGLLERV 169

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1731025460 842 IRLVLAYDESLSHWIYAASDMFIIPSIFEPCGLTQMIAMRYGSIPIVRKTGGLNDSVFD 900
Cdd:cd01635   170 VIIGGLVDDEVLELLLAAADVFVLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVD 228

CwlO1

COG3883

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...

108-329

1.07e-08

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

Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 58.30 E-value: 1.07e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 108 DTEGLNKGVQLEDLIGMIKSAEKNILLLNQARVRALEDLEKILSEKEELQREINGLEMRLAETDTRIEVAaqekvhVELL 187
Cdd:COG3883    15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEER------REEL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 188 EDQFEELQKQLNFSSGTVQSMN-GNLNDIpIDSLTKELHLLKSENIVLkNDIQTLKEELSNVK-NADQHLAFLEKERSVL 265
Cdd:COG3883    89 GERARALYRSGGSVSYLDVLLGsESFSDF-LDRLSALSKIADADADLL-EELKADKAELEAKKaELEAKLAELEALKAEL 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1731025460 266 ESSLKDLESKLSTSQEdgsKLSDLNAECMDLRNRVEHLQVLLDKATKQADQAIRVLQQNQELQE 329
Cdd:COG3883   167 EAAKAELEAQQAEQEA---LLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227

Glyco_trans_1_4

pfam13692

Glycosyl transferases group 1;

782-934

2.32e-08

Glycosyl transferases group 1;

Pssm-ID: 463957 [Multi-domain] Cd Length: 138 Bit Score: 53.67 E-value: 2.32e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 782 KPLVGCITRLVP-QKGIHLIRYAIYRTLELGG--QFVLLGSSPVPHIQREFEDIANHFQSHDQIRLVLAYdeslshwiYA 858
Cdd:pfam13692   1 RPVILFVGRLHPnVKGVDYLLEAVPLLRKRDNdvRLVIVGDGPEEELEELAAGLEDRVIFTGFVEDLAEL--------LA 72

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1731025460 859 ASDMFIIPSIFEPCGLTQMIAMRYGsIPIV-RKTGGLNDSVFDVddettptelqNGYTFLTPDEQGLNNALERAFSH 934
Cdd:pfam13692  73 AADVFVLPSLYEGFGLKLLEAMAAG-LPVVaTDVGGIPELVDGE----------NGLLVPPGDPEALAEAILRLLED 138

MAD

pfam05557

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

117-354

2.54e-08

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

Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 57.83 E-value: 2.54e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 117 QLE-DLIGMIKSAEKNILLLNQARVRALEDLEKILSEKEELQREINGLEMRLAETDT----RIEVAAQEKVHVELLEDQF 191
Cdd:pfam05557  13 QLQnEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEalreQAELNRLKKKYLEALNKKL 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 192 EELQKQLNFSSGTVQSMNGNLNDIPIDSLTKELHL--LKSENIVLKNDIQTLKEELSNVKNADQHLAFLEKERSVLESSL 269
Cdd:pfam05557  93 NEKESQLADAREVISCLKNELSELRRQIQRAELELqsTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRI 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 270 KDLESKLS----------TSQEDGSKLSDLNAECMDLRNRVEHLQvlldkaTKQADQAIrVLQQNQELQEKVEKLEESLE 339
Cdd:pfam05557 173 KELEFEIQsqeqdseivkNSKSELARIPELEKELERLREHNKHLN------ENIENKLL-LKEEVEDLKRKLEREEKYRE 245

                         250
                  ....*....|....*
gi 1731025460 340 KANVFKLSSEKLQQE 354
Cdd:pfam05557 246 EAATLELEKEKLEQE 260

YhaN

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

141-336

2.89e-08

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.86 E-value: 2.89e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 141 RALEDLEKILSEKEELQREINGLEMRLAETDTRIEVAAQEKvhvELLEDQFEELQKQLNFSsgtvqsmngnlndipidSL 220
Cdd:COG4717    71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAEL---EELREELEKLEKLLQLL-----------------PL 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 221 TKELHLLKSENIVLKNDIQTLKEELSNVKNADQHLAFLEKERSVLESSLKDLESKLSTSQEDgsKLSDLNAECMDLRNRV 300
Cdd:COG4717   131 YQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEE--ELQDLAEELEELQQRL 208

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1731025460 301 EHLQVLLDKAT---KQADQAIRVLQQNQELQEKVEKLEE 336
Cdd:COG4717   209 AELEEELEEAQeelEELEEELEQLENELEAAALEERLKE 247

PRK03918

DNA double-strand break repair ATPase Rad50;

117-408

2.96e-08

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.77 E-value: 2.96e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 117 QLEDLigmiKSAEKNILLLNQARVRALEDLEKILSEKEELQREINGLEMRLAETDTRIEvaaqekvhveLLEDQFEELQK 196
Cdd:PRK03918  156 GLDDY----ENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREIN----------EISSELPELRE 221

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 197 QLNFSSGTVQSMngnlndipiDSLTKELHLLKSENIVLKNDIQTLKEELsnvKNADQHLAFLEKERSVLESSLKDLEsKL 276
Cdd:PRK03918  222 ELEKLEKEVKEL---------EELKEEIEELEKELESLEGSKRKLEEKI---RELEERIEELKKEIEELEEKVKELK-EL 288

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 277 STSQEDGSKLSDLNAECMDLRNRVEHLqvlldkatkqadqAIRVLQQNQELQEKVEKLEESLEKANVFKLSSEKLQQENE 356
Cdd:PRK03918  289 KEKAEEYIKLSEFYEEYLDELREIEKR-------------LSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLE 355

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1731025460 357 LMQQKIDLLEDRLQSSDEELQSYIKLYQESVKEFQDTLDTIKKAsKKTATDE 408
Cdd:PRK03918  356 ELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKA-KEEIEEE 406

SMC_prok_B

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

116-340

5.27e-08

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.99 E-value: 5.27e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  116 VQLEDLIGMIKSAEKNILLLNQARVRALEDLEKILSEKEELQREINGLEMRLAEtdtrievaaqEKVHVELLEDQFEELQ 195
Cdd:TIGR02168  309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEE----------LEAELEELESRLEELE 378

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  196 KQLnfssgtvqsmngnlndipiDSLTKELHLLKSENIVLKNDIQTLKEELS----NVKNADQHLAFLEKERSvlESSLKD 271
Cdd:TIGR02168  379 EQL-------------------ETLRSKVAQLELQIASLNNEIERLEARLErledRRERLQQEIEELLKKLE--EAELKE 437

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1731025460  272 LESKLSTSQEDgskLSDLNAECMDLRNRVEHLQVLLDKATKQADQAIRVLQQNQELQEKVEKLEESLEK 340
Cdd:TIGR02168  438 LQAELEELEEE---LEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503

PRK03918

DNA double-strand break repair ATPase Rad50;

117-399

7.68e-08

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.61 E-value: 7.68e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 117 QLEDLIGMIKSAEKnillLNQARVRALEDLEKILSEKEELQREINGLEMRLAETDTRIEVAAQEKVHVELLEDQFEELQK 196
Cdd:PRK03918  277 ELEEKVKELKELKE----KAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEK 352

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 197 QLNFSSGTVQSMN------GNLNDI-------PIDSLTKELHLLKSENIVLKNDIQTLKEELSNvknadqhlafLEKERS 263
Cdd:PRK03918  353 RLEELEERHELYEeakakkEELERLkkrltglTPEKLEKELEELEKAKEEIEEEISKITARIGE----------LKKEIK 422

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 264 VLESSLKDLES---------KLSTSQEDGSKLSDLNAECMDLRNRVEHLQVLLDKATKQADQAIRVLQQ------NQELQ 328
Cdd:PRK03918  423 ELKKAIEELKKakgkcpvcgRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKeselikLKELA 502

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1731025460 329 EKVEKLEESLEKANVFKLssEKLQQENELMQQKIDLLEDRLQSSDEELQSyIKLYQESVKEFQDTLDTIKK 399
Cdd:PRK03918  503 EQLKELEEKLKKYNLEEL--EKKAEEYEKLKEKLIKLKGEIKSLKKELEK-LEELKKKLAELEKKLDELEE 570

SMC_prok_A

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

102-317

8.17e-08

Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 56.61 E-value: 8.17e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  102 EITGEVDTEGLNKGVQ----LEDLIGMIKSAEKNILLLNQ-------ARVRALEDLEKILSEKEELQREINGLEMRLAET 170
Cdd:TIGR02169  276 ELNKKIKDLGEEEQLRvkekIGELEAEIASLERSIAEKEReledaeeRLAKLEAEIDKLLAEIEELEREIEEERKRRDKL 355

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  171 DTRIEVAAQEKvhvELLEDQFEELQKQLNFSSGTVQSMNGNlndipIDSLTKELHLLKSENIVLKNDIQTLKEELSNVKN 250
Cdd:TIGR02169  356 TEEYAELKEEL---EDLRAELEEVDKEFAETRDELKDYREK-----LEKLKREINELKRELDRLQEELQRLSEELADLNA 427

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1731025460  251 A----DQHLAFLEKERSVLESSLKDLESKLSTSQEDGSK----LSDLNAECMDLRNRVEHLQVLLDKATKQADQA 317
Cdd:TIGR02169  428 AiagiEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKyeqeLYDLKEEYDRVEKELSKLQRELAEAEAQARAS 502

SMC_prok_B

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

106-342

1.26e-07

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.83 E-value: 1.26e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  106 EVDTEGLNKGVQLEDLIGMIKSAEKNILLLNQARVRALEDLEKILSEKEELQREINGLEMRLAETDtriEVAAQEKVHVE 185
Cdd:TIGR02168  814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALL---NERASLEEALA 890

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  186 LLEDQFEELQKQLNFSSGTVQSMNGNLndipiDSLTKELHLLKSENIVLKNDIQTLKEELSNV-----KNADQHLAFLEK 260
Cdd:TIGR02168  891 LLRSELEELSEELRELESKRSELRREL-----EELREKLAQLELRLEGLEVRIDNLQERLSEEysltlEEAEALENKIED 965

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  261 ERSVLESSLKDLESKLstsqedgSKLSDLNAECMD----LRNRVEHLqvlldkatkqadqairvLQQNQELQEKVEKLEE 336
Cdd:TIGR02168  966 DEEEARRRLKRLENKI-------KELGPVNLAAIEeyeeLKERYDFL-----------------TAQKEDLTEAKETLEE 1021


                   ....*.
gi 1731025460  337 SLEKAN 342
Cdd:TIGR02168 1022 AIEEID 1027

CALCOCO1

pfam07888

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...

108-385

2.13e-07

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: 54.52 E-value: 2.13e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 108 DTEGLNKGVQLEDLIGMIKSAEKNILLL----NQARVRALEDLEKILSEKEeLQREINgLEmRLAETdtrievaaQEKVH 183
Cdd:pfam07888  95 KHEELEEKYKELSASSEELSEEKDALLAqraaHEARIRELEEDIKTLTQRV-LERETE-LE-RMKER--------AKKAG 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 184 VELLEDQFE--ELQKQLNFSSGTVQSMNGNLNdipidSLTKELHLLKSENIVLKNDIQTLKEELSNvknADQHLAFLEKE 261
Cdd:pfam07888 164 AQRKEEEAErkQLQAKLQQTEEELRSLSKEFQ-----ELRNSLAQRDTQVLQLQDTITTLTQKLTT---AHRKEAENEAL 235

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 262 RSVLESSLKDLESKLSTSQEDGSKLSDLNAecmdLRNRVehlQVLLDKATKQADQA-IRVLQQNQELQEkvekleeslEK 340
Cdd:pfam07888 236 LEELRSLQERLNASERKVEGLGEELSSMAA----QRDRT---QAELHQARLQAAQLtLQLADASLALRE---------GR 299

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1731025460 341 ANvfklssekLQQENELMQQKIDLLEDRLQSSDEELQSYIKLYQE 385
Cdd:pfam07888 300 AR--------WAQERETLQQSAEADKDRIEKLSAELQRLEERLQE 336

PRK03918

DNA double-strand break repair ATPase Rad50;

118-340

3.15e-07

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.68 E-value: 3.15e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 118 LEDLIGMIKSAEKNILLLNqarvraLEDLEKILSEKEELQREINGLEMRLAETDTRIEVAAQEKVHVELLEDQFEELQKQ 197
Cdd:PRK03918  498 LKELAEQLKELEEKLKKYN------LEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEE 571

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 198 LnfssGTVQSMNGNLNDIPIDSLTKELHLLKS---ENIVLKNDIQTLKEELSNVKNADQHLAFLEKERSVLESSLKDLES 274
Cdd:PRK03918  572 L----AELLKELEELGFESVEELEERLKELEPfynEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRK 647

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1731025460 275 KLST-----SQEDGSKLSD----LNAECMDLRNRVEHLQVLLDKATKQADQAIRVLQQNQELQEKVEKLEESLEK 340
Cdd:PRK03918  648 ELEElekkySEEEYEELREeyleLSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALER 722

Glyco_transf_4

pfam13439

Glycosyltransferase Family 4;

500-741

3.60e-07

Glycosyltransferase Family 4;

Pssm-ID: 463877 [Multi-domain] Cd Length: 169 Bit Score: 50.99 E-value: 3.60e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 500 GGLGDVITGLSKALQSRGHLVEIVLPKYDcmeysrikdlrlldvvlesyfdGRLFKNKIWVGTVEGLPVYFiephhpdkf 579
Cdd:pfam13439   1 GGVERYVLELARALARRGHEVTVVTPGGP----------------------GPLAEEVVRVVRVPRVPLPL--------- 49

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 580 fwraqyygeHDDFKRFSYFSRAALELLLRAgkRPDIIHCHDWQTAFIAPLYWdlyypKGLNSARICFTCHNFEYqgtapa 659
Cdd:pfam13439  50 ---------PPRLLRSLAFLRRLRRLLRRE--RPDVVHAHSPFPLGLAALAA-----RLRLGIPLVVTYHGLFP------ 107

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 660 sdlascgldvdQLNRQDRLQDNSSHERINPVKGAVVFSNIVTTVSPTYAQEVRRAEGghglhstlnFHSKKFFGILNGID 739
Cdd:pfam13439 108 -----------DYKRLGARLSPLRRLLRRLERRLLRRADRVIAVSEAVADELRRLYG---------VPPEKIRVIPNGVD 167


                  ..
gi 1731025460 740 TD 741
Cdd:pfam13439 168 LE 169

Glycos_transf_1

pfam00534

Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...

782-948

6.43e-07

Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family.

Pssm-ID: 425737 [Multi-domain] Cd Length: 158 Bit Score: 49.97 E-value: 6.43e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 782 KPLVGCITRLVPQKGIHLIRYAIYRTLELGGQFVLL--GSSPVPhiQREFEDIANHFQSHDQIRLVLAYDESLSHwIYAA 859
Cdd:pfam00534   2 KKIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLViaGDGEEE--KRLKKLAEKLGLGDNVIFLGFVSDEDLPE-LLKI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 860 SDMFIIPSIFEPCGLTQMIAMRYGSIPIVRKTGGLNDSVfdvddettpTELQNGYTFLTPDEQGLNNALERAfshyLNNP 939
Cdd:pfam00534  79 ADVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVV---------KDGETGFLVKPNNAEALAEAIDKL----LEDE 145


                  ....*....
gi 1731025460 940 SSWQQLVQK 948
Cdd:pfam00534 146 ELRERLGEN 154

Taxilin

pfam09728

Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ...

220-408

9.60e-07

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

Pssm-ID: 462861 [Multi-domain] Cd Length: 302 Bit Score: 51.88 E-value: 9.60e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 220 LTKELHLLKSENIvlkndiQTLKEELSNVKNADQHLaflekersvlESSLKDLESKLSTSQEDGSKLSDLNaecMDLRNR 299
Cdd:pfam09728  79 LQKQNKKLKEESK------KLAKEEEEKRKELSEKF----------QSTLKDIQDKMEEKSEKNNKLREEN---EELREK 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 300 vehLQVLLDKATKQADQAIRVLQQNqELQEKVekLEESLEKANVFKlssEKLQQENElmQQKIDLLEDR---LQSSDEEL 376
Cdd:pfam09728 140 ---LKSLIEQYELRELHFEKLLKTK-ELEVQL--AEAKLQQATEEE---EKKAQEKE--VAKARELKAQvqtLSETEKEL 208

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1731025460 377 QSYIKLYQESVKEFQDTL-------DTIKKA----SKKTATDE 408
Cdd:pfam09728 209 REQLNLYVEKFEEFQDTLnksnevfTTFKKEmekmSKKIKKLE 251

YhaN

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

141-381

1.78e-06

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 1.78e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 141 RALEDLEKILSEKEELQREINGLEMRLAETDTRIEVAAQEKVHVELLEDQFEELQKQLNFSSGTVQSMNGNLNDIPIDSL 220
Cdd:COG4717   196 DLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTI 275

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 221 TK-----------ELHLLKSENIVLKNDIQTLK--EELSNVKNA--DQHLAFLEKERSVLESSLKDLESKLSTSQEDGSK 285
Cdd:COG4717   276 AGvlflvlgllalLFLLLAREKASLGKEAEELQalPALEELEEEelEELLAALGLPPDLSPEELLELLDRIEELQELLRE 355

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 286 LSDLNAEcMDLRNRVEHLQVLLDKAT----KQADQAIRVLQQNQELQEKVEKLEESLEKANVFKLSSEKLQQENELmQQK 361
Cdd:COG4717   356 AEELEEE-LQLEELEQEIAALLAEAGvedeEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEEL-EEE 433

                         250       260
                  ....*....|....*....|
gi 1731025460 362 IDLLEDRLQSSDEELQSYIK 381
Cdd:COG4717   434 LEELEEELEELEEELEELRE 453

rad50

TIGR00606

rad50; All proteins in this family for which functions are known are involvedin recombination, ...

104-409

2.76e-06

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).

Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 51.59 E-value: 2.76e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  104 TGEVDTEGLNKGV-QLEDLIGMIKSAE---KNILLLNQARVRALEDLEK----------------ILSEKEELQREINGL 163
Cdd:TIGR00606  441 TIELKKEILEKKQeELKFVIKELQQLEgssDRILELDQELRKAERELSKaeknsltetlkkevksLQNEKADLDRKLRKL 520

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  164 EMRLAETDTRIEVAAQEKVHVELLEDQFEELQKQLNFSSGTVQSMNGNLNDIPIdsLTKELHLLKSENIVLKNDIQTLKE 243
Cdd:TIGR00606  521 DQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQ--LEDWLHSKSKEINQTRDRLAKLNK 598

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  244 ELSNVKNADQHLAFLEKERSVLESSLKDLESKLSTSQEDGSKLSDLNAECMDLRNRV-----------EHLQVLLDKATK 312
Cdd:TIGR00606  599 ELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKSSKQRamlagatavysQFITQLTDENQS 678

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  313 QADQAIRVLQQNQELQEKVEKLEESLEKANVFKLSSE----KLQQENELMQQKIDLLEDRLQSSDEELQSYIKLYQESVK 388
Cdd:TIGR00606  679 CCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTEselkKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNR 758

                          330       340
                   ....*....|....*....|.
gi 1731025460  389 EFQDTLDTIKKASKKTATDEP 409
Cdd:TIGR00606  759 DIQRLKNDIEEQETLLGTIMP 779

GT4_MtfB-like

cd03809

glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...

751-965

3.30e-06

glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. MtfB (mannosyltransferase B) in E. coli has been shown to direct the growth of the O9-specific polysaccharide chain. It transfers two mannoses into the position 3 of the previously synthesized polysaccharide.

Pssm-ID: 340838 [Multi-domain] Cd Length: 362 Bit Score: 50.44 E-value: 3.30e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 751 IKVQYNANDLQ-GKAENKDALRRHLGLssnvRKPLVGCITRLVPQKGIH-LIR-YAIYRTLELGGQFVLLGSSPvpHIQR 827
Cdd:cd03809   164 IVVIPLGVDPSfFPPESAAVLIAKYLL----PEPYFLYVGTLEPRKNHErLLKaFALLKKQGGDLKLVIVGGKG--WEDE 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 828 EFEDIANHFQSHDQIRLvLAY--DESLsHWIYAASDMFIIPSIFEPCGLTQMIAMRYGsIPIVrktgGLNDSVFdvddet 905
Cdd:cd03809   238 ELLDLVKKLGLGGRVRF-LGYvsDEDL-PALYRGARAFVFPSLYEGFGLPVLEAMACG-TPVI----ASNISVL------ 304

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1731025460 906 tPTELQNGYTFLTP-DEQGLNNALERAfshyLNNPSSWQQLVQKVMD--VDFSWETSAAQYEE 965
Cdd:cd03809   305 -PEVAGDAALYFDPlDPESIADAILRL----LEDPSLREELIRKGLEraKKFSWEKTAEKTLE 362

SCP-1

pfam05483

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...

84-403

3.44e-06

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.

Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 51.26 E-value: 3.44e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  84 SAVQHNTEKEVSGMTapgEITGEvDTEGLNKGVQLEDLIGMIKSAEKNILLLNQARVRALEDLE----KILSEKEELQRE 159
Cdd:pfam05483 397 TKFKNNKEVELEELK---KILAE-DEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEiqltAIKTSEEHYLKE 472

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 160 INGLEMRLA-ETDTRIEVAAqekvHVELLEDQFEELQKQlnfSSGTVQSMNGNLNDIpIDSLTKELHLLKSenivlkndI 238
Cdd:pfam05483 473 VEDLKTELEkEKLKNIELTA----HCDKLLLENKELTQE---ASDMTLELKKHQEDI-INCKKQEERMLKQ--------I 536

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 239 QTLKEELSNVKNAdqhlafLEKERSVLESSLKDLESKLSTSQEDGSKLSDLNAECMDLRNRVEHLQVLLDKATKQADQAI 318
Cdd:pfam05483 537 ENLEEKEMNLRDE------LESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNI 610

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 319 RVLQQ-NQELQEKVEKLEESLekaNVFKLSSEKLQQENELMQQKIDLLEDRLQSSDEELQSYIKLYQESVKEFQDTLDTI 397
Cdd:pfam05483 611 EELHQeNKALKKKGSAENKQL---NAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEA 687


                  ....*.
gi 1731025460 398 KKASKK 403
Cdd:pfam05483 688 VKLQKE 693

YhaN

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

117-413

4.49e-06

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 4.49e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 117 QLEDLIGMIKSAEKNILLLNQ--ARVRALEDLEKILSEKEELQREINGLEMRLAETDTRIEVAAQEKVHVELLEDQFEEL 194
Cdd:COG4717    96 ELEELEEELEELEAELEELREelEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAEL 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 195 QKQLN-----FSSGTVQSMNGNLNDipIDSLTKELHLLKSENIVLKNDIQTLKEELSNVKNADQHLAFLEK--------- 260
Cdd:COG4717   176 QEELEelleqLSLATEEELQDLAEE--LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERlkearllll 253

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 261 ---------------------------------------------------ERSVLESSLKDLESK--LSTSQEDGSKLS 287
Cdd:COG4717   254 iaaallallglggsllsliltiagvlflvlgllallflllarekaslgkeaEELQALPALEELEEEelEELLAALGLPPD 333

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 288 DLNAECMDLRNRVEHLQVLLDKATKQADQA-IRVLQQNQ-------------ELQEKVEKLEESLEKANVFKLSSEKLQQ 353
Cdd:COG4717   334 LSPEELLELLDRIEELQELLREAEELEEELqLEELEQEIaallaeagvedeeELRAALEQAEEYQELKEELEELEEQLEE 413

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1731025460 354 ENELMQQKIDLL-EDRLQSSDEELQSYIKLYQESVKEFQDTLDTIKKASKKTATDEPVNDM 413
Cdd:COG4717   414 LLGELEELLEALdEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAEL 474

GT4_WbnK-like

cd03807

Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...

720-967

4.79e-06

Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. WbnK in Shigella dysenteriae has been shown to be involved in the type 7 O-antigen biosynthesis.

Pssm-ID: 340836 [Multi-domain] Cd Length: 362 Bit Score: 50.01 E-value: 4.79e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 720 LHSTLNFHSKKFFGILNGIDTDVWNPStdsfikvqynandlqgkAENKDALRRHLGLSSNVRkpLVGCITRLVPQKGIHL 799
Cdd:cd03807   147 FHQEQGYAKNKIVVIYNGIDLFKLSPD-----------------DASRARARRRLGLAEDRR--VIGIVGRLHPVKDHSD 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 800 IRYAIYRTLELGGQ--FVLLGSSPV-PHIQREFEDIAN----HF--QSHDQIRLvlaydeslshwiYAASDMFIIPSIFE 870
Cdd:cd03807   208 LLRAAALLVETHPDlrLLLVGRGPErPNLERLLLELGLedrvHLlgERSDVPAL------------LPAMDIFVLSSRTE 275

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 871 PCGLTQMIAMRYGsIPIV-RKTGGLNDSVFDVDDETTPTElqngytfltpDEQGLNNALERAfshyLNNPSSWQQLV--- 946
Cdd:cd03807   276 GFPNALLEAMACG-LPVVaTDVGGAAELVDDGTGFLVPAG----------DPQALADAIRAL----LEDPEKRARLGraa 340

                         250       260
                  ....*....|....*....|..
gi 1731025460 947 -QKVMDvDFSWETSAAQYEELY 967
Cdd:cd03807   341 rERIAN-EFSIDAMVRRYETLY 361

CwlO1

COG3883

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...

132-415

7.53e-06

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

Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.44 E-value: 7.53e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 132 ILLLNQARVRALEDLEKILSEKEELQREINGLEMRLAETDTRIEVAAQEkvhVELLEDQFEELQKQlnfssgtvqsmngn 211
Cdd:COG3883     4 LALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEE---YNELQAELEALQAE-------------- 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 212 lndipIDSLTKELHLLKsENIVLKNDIqtLKEELSNVKNADQHLAFLEkerSVLES-SLKDLESKLSTSqedgSKLSDLN 290
Cdd:COG3883    67 -----IDKLQAEIAEAE-AEIEERREE--LGERARALYRSGGSVSYLD---VLLGSeSFSDFLDRLSAL----SKIADAD 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 291 AECMDlrnRVEHLQVLLDKATKQADQAIrvlqqnQELQEKVEKLEESLEKANvfKLSSEKLQQENELMQQKIDLLE--DR 368
Cdd:COG3883   132 ADLLE---ELKADKAELEAKKAELEAKL------AELEALKAELEAAKAELE--AQQAEQEALLAQLSAEEAAAEAqlAE 200

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1731025460 369 LQSSDEELQSYIKLYQESVKEFQDTLDTIKKASKKTATDEPVNDMPW 415
Cdd:COG3883   201 LEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAA 247

HOOK

pfam05622

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...

148-395

1.04e-05

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.

Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 49.30 E-value: 1.04e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 148 KILSEK-EELQREINGLemrLAETDTrievaaqekvhvelLEDQFEELQ-KQLNFSSGTVQSMNGNLNDIPIDSLTKELH 225
Cdd:pfam05622 214 KKLEEKlEALQKEKERL---IIERDT--------------LRETNEELRcAQLQQAELSQADALLSPSSDPGDNLAAEIM 276

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 226 ---------LLKSENIVLKndiqtLKEELSNvknaDQHLAFLEKERSVLESSLKDLESKLSTSQEdgsklsdlnaECMDL 296
Cdd:pfam05622 277 paeirekliRLQHENKMLR-----LGQEGSY----RERLTELQQLLEDANRRKNELETQNRLANQ----------RILEL 337

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 297 RNRVEHLQVLLDKATKQADQAIRVLQQNQELQEKVEKLEESLEKAnvfKLSSEKLQQENEL-MQQKIDLLEDRLQSSDEE 375
Cdd:pfam05622 338 QQQVEELQKALQEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQKK---KEQIEELEPKQDSnLAQKIDELQEALRKKDED 414

                         250       260
                  ....*....|....*....|...
gi 1731025460 376 LQSY---IKLYQESVKEFQDTLD 395
Cdd:pfam05622 415 MKAMeerYKKYVEKAKSVIKTLD 437

COG4372

Uncharacterized protein, contains DUF3084 domain [Function unknown];

117-385

1.25e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];

Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.75 E-value: 1.25e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 117 QLEDLIGMIKSAEKNILLLNQARVRALEDLEKILSEKEELQREINGLEMRLAETDTRIEVAAQEKvhvELLEDQFEELQK 196
Cdd:COG4372    46 ELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEA---EELQEELEELQK 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 197 QLNFSSGTVQSMNGNlndipIDSLTKELHLLKSENIVLKNDIQTLKEELSNVKNADQHLAfLEKERSVLESSLKDLESKL 276
Cdd:COG4372   123 ERQDLEQQRKQLEAQ-----IAELQSEIAEREEELKELEEQLESLQEELAALEQELQALS-EAEAEQALDELLKEANRNA 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 277 STSQEDGSKLSDLNAECMDLRNRVEHLQVLLDKATKQADQAIRVLQQNQELQEKVEKLEESLEKANVFKLSSEKLQQENE 356
Cdd:COG4372   197 EKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEE 276

                         250       260
                  ....*....|....*....|....*....
gi 1731025460 357 LMQQKIDLLEDRLQSSDEELQSYIKLYQE 385
Cdd:COG4372   277 ELEIAALELEALEEAALELKLLALLLNLA 305

rad50

TIGR00606

rad50; All proteins in this family for which functions are known are involvedin recombination, ...

145-444

1.36e-05

Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 49.27 E-value: 1.36e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  145 DLEKILSEKEELQREINGLEMRLAETDTRIEVAAQEKVHVELLEDQFEELQKQLNFSSGTVQSMNGNLNDI--PIDSLTK 222
Cdd:TIGR00606  640 DLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKlkSTESELK 719

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  223 ELHLLKSENIVL----KNDIQTLKEELSNVKNADQHLAF--------LEKERSVLESSLKDLESKlSTSQEDGSKLSDLN 290
Cdd:TIGR00606  720 KKEKRRDEMLGLapgrQSIIDLKEKEIPELRNKLQKVNRdiqrlkndIEEQETLLGTIMPEEESA-KVCLTDVTIMERFQ 798

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  291 AECMDLRNRVEHLQVLLDKAtkqaDQAIRVLQQNQELQEKVEKLEESLEKANVFKLSSEKLQQENELMQQKIDLLEDRLQ 370
Cdd:TIGR00606  799 MELKDVERKIAQQAAKLQGS----DLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKL 874

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1731025460  371 SSDEELQSYIKLYQESVKEFQDTLDTIKKASKKTATDEPVNDMPWEFWSRLLLLIDGWLLEEKISGDDAKLLKE 444
Cdd:TIGR00606  875 QIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKE 948

Mplasa_alph_rch

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...

130-403

1.60e-05

Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.86 E-value: 1.60e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 130 KNILLLNQARVRALED-LEKILSEKEELQREINGLEMRLAETDTRIEVaaqekvhvelLEDQFEELQKQLNfssgtvqSM 208
Cdd:TIGR04523  25 KNIANKQDTEEKQLEKkLKTIKNELKNKEKELKNLDKNLNKDEEKINN----------SNNKIKILEQQIK-------DL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 209 NGNL--NDIPIDSLTKELHLLKSENIVLKNDIQTLKEELSNVK----NADQHLAFLEKERSVLESSLKDLEsklstsqed 282
Cdd:TIGR04523  88 NDKLkkNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEkqkkENKKNIDKFLTEIKKKEKELEKLN--------- 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 283 gSKLSDLNAECMDLRNrvEHLQVLLDKATKQADQAIRVLQQNQE------LQEKVEKLEESLEKANVFKLSSEKLQQENE 356
Cdd:TIGR04523 159 -NKYNDLKKQKEELEN--ELNLLEKEKLNIQKNIDKIKNKLLKLelllsnLKKKIQKNKSLESQISELKKQNNQLKDNIE 235

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1731025460 357 LMQQKIDLLEDRLQSSDEELQSYIKLYQESVKEFQDTLDTIKKASKK 403
Cdd:TIGR04523 236 KKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKK 282

GAS

pfam13851

Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...

187-343

1.73e-05

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: 46.82 E-value: 1.73e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 187 LEDQFEELQKQlnfssgtvqsmngnlndipIDSLTKELHLLKSENIVLKNDIQTLKEElsnVKNADQHLAFLEKERSvle 266
Cdd:pfam13851  31 LKEEIAELKKK-------------------EERNEKLMSEIQQENKRLTEPLQKAQEE---VEELRKQLENYEKDKQ--- 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 267 sSLKDLESKLSTSQEdgsKLSDLNAECMDLRNRVEHLQVLLDKATKQADQAIRVLQQ-----NQELQEKVEKLEESLEKA 341
Cdd:pfam13851  86 -SLKNLKARLKVLEK---ELKDLKWEHEVLEQRFEKVERERDELYDKFEAAIQDVQQktglkNLLLEKKLQALGETLEKK 161


                  ..
gi 1731025460 342 NV 343
Cdd:pfam13851 162 EA 163

PRK02224

DNA double-strand break repair Rad50 ATPase;

142-400

1.78e-05

DNA double-strand break repair Rad50 ATPase;

Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.88 E-value: 1.78e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 142 ALEDLEKILSEKEE--LQREINGLEMRLAETDTRIE-------VAAQEKVHVELLEDQFEELQKQLNfssgTVQSmngnl 212
Cdd:PRK02224  188 SLDQLKAQIEEKEEkdLHERLNGLESELAELDEEIEryeeqreQARETRDEADEVLEEHEERREELE----TLEA----- 258

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 213 ndiPIDSLTKELHLLKSENIVLKNDIQTLKEELSNvknadqhlafLEKERSVLESSLkDLESKLSTSQEDgsKLSDLNAE 292
Cdd:PRK02224  259 ---EIEDLRETIAETEREREELAEEVRDLRERLEE----------LEEERDDLLAEA-GLDDADAEAVEA--RREELEDR 322

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 293 CMDLRNRVEHLQVLLDKATKQAD----QAIRVLQQNQELQEKVEKLEESLEKAnvfKLSSEKLQQENELMQQKIDLLEDR 368
Cdd:PRK02224  323 DEELRDRLEECRVAAQAHNEEAEslreDADDLEERAEELREEAAELESELEEA---REAVEDRREEIEELEEEIEELRER 399

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1731025460 369 LQSSD---EELQSYIKLYQE-------SVKEFQDTLDTIKKA 400
Cdd:PRK02224  400 FGDAPvdlGNAEDFLEELREerdelreREAELEATLRTARER 441

SMC_prok_A

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

113-336

1.97e-05

Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.91 E-value: 1.97e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  113 NKGVQLEDLIGMIKSAEKNILLLNQARVRALEDLEKILSEKEELQREINGLEMRLAETDTRIEvaaQEKVHVELLEDQFE 192
Cdd:TIGR02169  795 EIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIE---NLNGKKEELEEELE 871

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  193 ELQKQLNfssgtvqSMNGNLNDipidsLTKELHLLKSENIVLKNDIQTLKEElsnVKNADQHLAFLEKERSVLESSLKDL 272
Cdd:TIGR02169  872 ELEAALR-------DLESRLGD-----LKKERDELEAQLRELERKIEELEAQ---IEKKRKRLSELKAKLEALEEELSEI 936

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1731025460  273 ESKLSTSQEDGSKLSDLNAECMDLRNRVEHLQVLLDKATKQADQAIRVLQQNQELQEKVEKLEE 336
Cdd:TIGR02169  937 EDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEE 1000

CALCOCO1

pfam07888

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...

129-377

3.47e-05

Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 47.58 E-value: 3.47e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 129 EKNILLlnQARVRALEDLEKILSE----KEELQREINGLEMRLAETDTRIEVAAQEkvHVELledqfEELQKQLNFSSGT 204
Cdd:pfam07888  42 ERAELL--QAQEAANRQREKEKERykrdREQWERQRRELESRVAELKEELRQSREK--HEEL-----EEKYKELSASSEE 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 205 VQSMNGNLNDIPIDSLTKELHLlksenivlKNDIQTLKE-------ELSNVKNADQHLAFLEKERsvlESSLKDLESKLS 277
Cdd:pfam07888 113 LSEEKDALLAQRAAHEARIREL--------EEDIKTLTQrvleretELERMKERAKKAGAQRKEE---EAERKQLQAKLQ 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 278 TSQEDGSKLS-----------DLNAECMDLRNRVEHLQVLLDKATKQADQAIRVLQQNQELQEKVEKLEESLE--KANVF 344
Cdd:pfam07888 182 QTEEELRSLSkefqelrnslaQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEglGEELS 261

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1731025460 345 KLSSEKLQQENELMQQKIDLLEDRLQSSDEELQ 377
Cdd:pfam07888 262 SMAAQRDRTQAELHQARLQAAQLTLQLADASLA 294

COG1340

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

144-408

3.62e-05

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

Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.83 E-value: 3.62e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 144 EDLEKILSEKEELQREINGLEMRLAETDTRIEVAAQEKvhvELLEDQFEELQKQLNfssgTVQSMngnlndipIDSLTKE 223
Cdd:COG1340     8 SSLEELEEKIEELREEIEELKEKRDELNEELKELAEKR---DELNAQVKELREEAQ----ELREK--------RDELNEK 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 224 LHLLKSENIVLKNDIQTLKEELSNVKNADQHLAFLEKERSVLESSLKDLESKLSTSQedgsklSDLNAEcMDLRNRVEHL 303
Cdd:COG1340    73 VKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEV------LSPEEE-KELVEKIKEL 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 304 QVLLDKATKQADQA---IRVLQQNQELQEKVEKLEESL----EKANVFKLSSEKLQQENELMQQKIDLL----EDRLQSS 372
Cdd:COG1340   146 EKELEKAKKALEKNeklKELRAELKELRKEAEEIHKKIkelaEEAQELHEEMIELYKEADELRKEADELhkeiVEAQEKA 225

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1731025460 373 DEELQSYIKLyQESVKEFQDTLDTIKKASKKTATDE 408
Cdd:COG1340   226 DELHEEIIEL-QKELRELRKELKKLRKKQRALKREK 260

GT4-like

cd03814

glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...

737-898

3.83e-05

glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family of glycosyltransferases and includes a sequence annotated as alpha-D-mannose-alpha(1-6)phosphatidyl myo-inositol monomannoside transferase from Bacillus halodurans. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria and eukaryotes.

Pssm-ID: 340842 [Multi-domain] Cd Length: 365 Bit Score: 46.90 E-value: 3.83e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 737 GIDTDVWNPSTDSFikvqynandlqgkaenkdALRRHLGLSSnvrKPLVGCITRLVPQKGIHLIRYAIYR-TLELGGQFV 815
Cdd:cd03814   174 GVDTELFHPSRRDA------------------ALRRRLGPPG---RPLLLYVGRLAPEKNLEALLDADLPlAASPPVRLV 232

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 816 LLGSSPV-PHIQREFEDIanHFqshdqirLVLAYDESLSHwIYAASDMFIIPSIFEPCGLTQMIAMRYGsIP-IVRKTGG 893
Cdd:cd03814   233 VVGDGPArAELEARGPDV--IF-------TGFLTGEELAR-AYASADVFVFPSRTETFGLVVLEAMASG-LPvVAADAGG 301


                  ....*
gi 1731025460 894 LNDSV 898
Cdd:cd03814   302 PRDIV 306

SCP-1

pfam05483

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...

129-446

4.28e-05

Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 47.41 E-value: 4.28e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 129 EKNILLLNQARVRA-----------LEDLEKILSEKEELQREINGLEMRLaetdTRIEVAAQEKvhvellEDQFEELQKQ 197
Cdd:pfam05483 193 EKMILAFEELRVQAenarlemhfklKEDHEKIQHLEEEYKKEINDKEKQV----SLLLIQITEK------ENKMKDLTFL 262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 198 LNFSSGTVQSMngnlndipidsltKELHLLKSENIVLKNDIQT-LKEELSNVKnadqhlafLEKERSVleSSLKDLESKL 276
Cdd:pfam05483 263 LEESRDKANQL-------------EEKTKLQDENLKELIEKKDhLTKELEDIK--------MSLQRSM--STQKALEEDL 319

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 277 STSQEDGSKLSDLNAECMDLRN--RVEHLQVL--LDKATKQADQAIRVLQQ------------NQELQEKVEKLEESLEK 340
Cdd:pfam05483 320 QIATKTICQLTEEKEAQMEELNkaKAAHSFVVteFEATTCSLEELLRTEQQrleknedqlkiiTMELQKKSSELEEMTKF 399

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 341 ANVFKLSSEKLQQ---ENELM---QQKIDLLEDRLQSSDEELQSYIKLYQESVKEFQDTLdTIKKASKKTATDEpVNDMP 414
Cdd:pfam05483 400 KNNKEVELEELKKilaEDEKLldeKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQL-TAIKTSEEHYLKE-VEDLK 477

                         330       340       350
                  ....*....|....*....|....*....|..
gi 1731025460 415 WEFWSRLLLLIDGWLLEEKISGDDAKLLKEMA 446
Cdd:pfam05483 478 TELEKEKLKNIELTAHCDKLLLENKELTQEAS 509

Laminin_I

pfam06008

Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ...

142-400

4.62e-05

Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.

Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 46.25 E-value: 4.62e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 142 ALEDLEKILSEKEELQREINGLEMRLAETDTRIEVAAQEkvhVELLEDQFEELQKQLNFSSGTVQSMNGNLNDI--PIDS 219
Cdd:pfam06008  10 ALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKE---LSSLAQETEELQKKATQTLAKAQQVNAESERTlgHAKE 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 220 LTKELHLLKSENIVLKNDIQTLKEELSNVKNADqhlafLEKERSVLESSLKDLESKLSTSQEDGSKLSDLNAEcmDLRNR 299
Cdd:pfam06008  87 LAEAIKNLIDNIKEINEKVATLGENDFALPSSD-----LSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQ--DLLSR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 300 VEHLQVLLDKATKQADQAIRvlQQNQELQEKVEKLEESLEKANVFKLSSEKLQQENELMQQKIDLLEDRLQSSDEELQSY 379
Cdd:pfam06008 160 IQTWFQSPQEENKALANALR--DSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEET 237

                         250       260
                  ....*....|....*....|.
gi 1731025460 380 IKLYQESVKEFQDTLDTIKKA 400
Cdd:pfam06008 238 LKTARDSLDAANLLLQEIDDA 258

EzrA

pfam06160

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...

143-399

4.89e-05

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.

Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 47.16 E-value: 4.89e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 143 LEDLEKILSEKEEL---------QREINGLEMRLAETDTRI-----------EVAAQEKVHVELLEDQFEELQKQL---N 199
Cdd:pfam06160  62 LPDIEELLFEAEELndkyrfkkaKKALDEIEELLDDIEEDIkqileeldellESEEKNREEVEELKDKYRELRKTLlanR 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 200 FSSG-TVQSMNGNLNDIPID-----SLTKELHLLKSENIV--LKNDIQTLKEELSNVKnadqhlAFLEKERSVLESSLKD 271
Cdd:pfam06160 142 FSYGpAIDELEKQLAEIEEEfsqfeELTESGDYLEAREVLekLEEETDALEELMEDIP------PLYEELKTELPDQLEE 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 272 LESKLSTSQEDGSKLSDLN--AECMDLRNRVEHLQVLLDK----ATKQADQAI--------------------------- 318
Cdd:pfam06160 216 LKEGYREMEEEGYALEHLNvdKEIQQLEEQLEENLALLENleldEAEEALEEIeeridqlydllekevdakkyveknlpe 295

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 319 ------RVLQQNQELQEKVEKLEESlekanvFKLSSEKLQQENELmQQKIDLLEDRLQSSDEEL----QSYIKLyQESVK 388
Cdd:pfam06160 296 iedyleHAEEQNKELKEELERVQQS------YTLNENELERVRGL-EKQLEELEKRYDEIVERLeekeVAYSEL-QEELE 367

                         330
                  ....*....|.
gi 1731025460 389 EFQDTLDTIKK 399
Cdd:pfam06160 368 EILEQLEEIEE 378

GT4_WlbH-like

cd03798

Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...

567-969

4.95e-05

Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Staphylococcus aureus CapJ may be involved in capsule polysaccharide biosynthesis. WlbH in Bordetella parapertussis has been shown to be required for the biosynthesis of a trisaccharide that, when attached to the B. pertussis lipopolysaccharide (LPS) core (band B), generates band A LPS.

Pssm-ID: 340828 [Multi-domain] Cd Length: 376 Bit Score: 46.60 E-value: 4.95e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 567 PVYFIEPHHpdkFFWRAQYYGehddfkrFSYFSRAALELLLRAGKRPDIIHCH-DWQTAFIAPLYwdlyypKGLNSARIC 645
Cdd:cd03798    60 PRDGRRLLP---LKPRLRLLA-------PLRAPSLAKLLKRRRRGPPDLIHAHfAYPAGFAAALL------ARLYGVPYV 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 646 FTCHnfeyqgtapASDLAscGLDVDQLNRQDRLQDNSSHERinpvkgavvfsniVTTVSPTYAQEVRRaegghglhstLN 725
Cdd:cd03798   124 VTEH---------GSDIN--VFPPRSLLRKLLRWALRRAAR-------------VIAVSKALAEELVA----------LG 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 726 FHSKKFFGILNGIDTDVWNPSTDsfikvqynandlqgkaenkdalRRHLGLSSnvrkPLVGCITRLVPQKGIH-LIR-YA 803
Cdd:cd03798   170 VPRDRVDVIPNGVDPARFQPEDR----------------------GLGLPLDA----FVILFVGRLIPRKGIDlLLEaFA 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 804 IYRTLELGGQFVLLGSSPvphiQRE-FEDIANHFQSHDQIRLV--LAYDEsLSHWiYAASDMFIIPSIFEPCGLTQMIAM 880
Cdd:cd03798   224 RLAKARPDVVLLIVGDGP----LREaLRALAEDLGLGDRVTFTgrLPHEQ-VPAY-YRACDVFVLPSRHEGFGLVLLEAM 297

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 881 RYGsIPIV-RKTGGLNDSVfdvddeTTPTelqNGYTFLTPDEQGLNNALERAfshyLNNP---SSWQQLVQKVMDvDFSW 956
Cdd:cd03798   298 ACG-LPVVaTDVGGIPEVV------GDPE---TGLLVPPGDADALAAALRRA----LAEPylrELGEAARARVAE-RFSW 362

                         410
                  ....*....|...
gi 1731025460 957 ETSAAQYEELYSK 969
Cdd:cd03798   363 VKAADRIAAAYRD 375

Cast

pfam10174

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...

148-407

5.49e-05

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: 47.12 E-value: 5.49e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 148 KILSEKEELQREINGLEMRLAETDTRIEVAAQEKVHV--------ELLED--QFEELQKQLNFSSGTVQSMNGNLNDipi 217
Cdd:pfam10174 175 KSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLreelhrrnQLQPDpaKTKALQTVIEMKDTKISSLERNIRD--- 251

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 218 dsLTKELHLLKSENIVLKNDIQtlkEELSNVKNADQHLAFLEKERSVLESSLKDLESKLSTSQedgSKLSDLNAECMDLR 297
Cdd:pfam10174 252 --LEDEVQMLKTNGLLHTEDRE---EEIKQMEVYKSHSKFMKNKIDQLKQELSKKESELLALQ---TKLETLTNQNSDCK 323

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 298 nrvEHLQVLLDKATKQaDQAIRVLQ-QNQELQEKVEKLEESLEKAN--VFKLSSEKLQQENEL--MQQKIDLLEDRLQSs 372
Cdd:pfam10174 324 ---QHIEVLKESLTAK-EQRAAILQtEVDALRLRLEEKESFLNKKTkqLQDLTEEKSTLAGEIrdLKDMLDVKERKINV- 398

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1731025460 373 deeLQSYIKLYQESVKEFQDTLDTIKKASKKTATD 407
Cdd:pfam10174 399 ---LQKKIENLQEQLRDKDKQLAGLKERVKSLQTD 430

Myosin_tail_1

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

117-407

5.72e-05

Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 47.09 E-value: 5.72e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  117 QLEDLIGMIKSAEKNILLLNQARVRALEDL--EKILSEKEELQREINGLEMRLAET---DTRIEVAAQEKVHVELlEDQF 191
Cdd:pfam01576  251 RLEEETAQKNNALKKIRELEAQISELQEDLesERAARNKAEKQRRDLGEELEALKTeleDTLDTTAAQQELRSKR-EQEV 329

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  192 EELQKQLNFSSGT----VQSMNGNLNDIpIDSLTKELHLLKSENIVLKNDIQTLKEELSN----VKNADQHLAFLEKERS 263
Cdd:pfam01576  330 TELKKALEEETRSheaqLQEMRQKHTQA-LEELTEQLEQAKRNKANLEKAKQALESENAElqaeLRTLQQAKQDSEHKRK 408

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  264 VLESSLKDLESKLSTS----QEDGSKLSDLNAECMDLRNRVEHLQVLLDKATKQADQAIRVLQQNQELQEkveklEESLE 339
Cdd:pfam01576  409 KLEGQLQELQARLSESerqrAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQ-----EETRQ 483

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1731025460  340 KANvfkLSSEKLQQENEL--MQQKIDLLEDRLQSSDEELQSYIKLYQESVKEFQD---TLDTIKKASKKTATD 407
Cdd:pfam01576  484 KLN---LSTRLRQLEDERnsLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEdagTLEALEEGKKRLQRE 553

GAS

pfam13851

Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...

232-381

6.23e-05

Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 44.90 E-value: 6.23e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 232 IVLKN--DIQTLKEELSNVKNADQH----LAFLEKERSVLESSLKDLESKLstsQEDGSKLSDLNAECMDLRN---RVEH 302
Cdd:pfam13851  20 ITRNNleLIKSLKEEIAELKKKEERneklMSEIQQENKRLTEPLQKAQEEV---EELRKQLENYEKDKQSLKNlkaRLKV 96

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1731025460 303 LQVLLDKATKQADQairVLQQNQELQEKVEKLEESLEKAnVFKLsSEKLQQENELMQQKIDLLEDRLQSSDEELQSYIK 381
Cdd:pfam13851  97 LEKELKDLKWEHEV---LEQRFEKVERERDELYDKFEAA-IQDV-QQKTGLKNLLLEKKLQALGETLEKKEAQLNEVLA 170

COG4372

Uncharacterized protein, contains DUF3084 domain [Function unknown];

117-403

7.76e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];

Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.05 E-value: 7.76e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 117 QLEDLIGMIKSAEKNILLLNQARVRALEDLEKILSEKEELQREINGLEMRLAETDTRIEVAAQEKvhvELLEDQFEELQK 196
Cdd:COG4372    88 QLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEEL---KELEEQLESLQE 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 197 QLNFSSGTVQSMNGNLNDIPIDSLTKELHLLKSENIVLKNDIQTLKEELSNVKNADQHLAFLEKERSVLESSLKDLESKL 276
Cdd:COG4372   165 ELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALEL 244

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 277 STSQEDGSKLSDLNaecmdlrnrVEHLQVLLDKATKQADQAIRVLQQNQELQEKVEKLEESLEKANVFKLSSEKLQQENE 356
Cdd:COG4372   245 EEDKEELLEEVILK---------EIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALED 315

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1731025460 357 LMQQKIDLLEDRLQSSDEELQSYIKLYQESVKEFQDTLDTIKKASKK 403
Cdd:COG4372   316 ALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKG 362

GumC

COG3206

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

117-317

7.78e-05

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

Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.55 E-value: 7.78e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 117 QLEDLIGMIKSAEKNIL-LLNQARVRALEDLEKILSEK-EELQREINGLEMRLAEtdtrievaaqekvhvelLEDQFEEL 194
Cdd:COG3206   183 QLPELRKELEEAEAALEeFRQKNGLVDLSEEAKLLLQQlSELESQLAEARAELAE-----------------AEARLAAL 245

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 195 QKQLNFSSGTVQSMngnLNDIPIDSLTKELHLLKSENIVLKN-------DIQTLKEELSNVKN-----ADQHLAFLEKER 262
Cdd:COG3206   246 RAQLGSGPDALPEL---LQSPVIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAqlqqeAQRILASLEAEL 322

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1731025460 263 SVLESSLKDLESKLSTSQEDGSKLSDLNAECMDLRNRVEHLQVLLDKATKQADQA 317
Cdd:COG3206   323 EALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEA 377

Cast

pfam10174

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...

142-371

8.77e-05

Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 46.35 E-value: 8.77e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 142 ALEDLEKILSEKE-ELQREINGLEMRLAETDTRIEVAAQEKVhVELLEDQFEELQKQLNFSSGTVQSM--NGNLNDIPID 218
Cdd:pfam10174 193 QLGHLEVLLDQKEkENIHLREELHRRNQLQPDPAKTKALQTV-IEMKDTKISSLERNIRDLEDEVQMLktNGLLHTEDRE 271

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 219 SLTKELHLLKSENIVLKNDIQTLKEELS----------------NVKNAD--QHLaflekerSVLESSLKDLESKLSTsq 280
Cdd:pfam10174 272 EEIKQMEVYKSHSKFMKNKIDQLKQELSkkesellalqtkletlTNQNSDckQHI-------EVLKESLTAKEQRAAI-- 342

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 281 edgsklsdLNAECMDLRNRVEHLQVLLDKATKQadqairvLQQNQE----LQEKVEKLEESLE----KANVFKLSSEKLQ 352
Cdd:pfam10174 343 --------LQTEVDALRLRLEEKESFLNKKTKQ-------LQDLTEekstLAGEIRDLKDMLDvkerKINVLQKKIENLQ 407

                         250
                  ....*....|....*....
gi 1731025460 353 QENELMQQKIDLLEDRLQS 371
Cdd:pfam10174 408 EQLRDKDKQLAGLKERVKS 426

CALCOCO1

pfam07888

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...

222-409

9.57e-05

Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 46.04 E-value: 9.57e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 222 KELHLLKSENIVLKNDIQTLKEELSNVKNAdqhlafLEKERSVLESSLKDLESKLSTSQEDGSKLSDLNAECMDLRNRVE 301
Cdd:pfam07888  41 QERAELLQAQEAANRQREKEKERYKRDREQ------WERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELS 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 302 HLQVLLDKATKQADQAIRVLQQN-QELQEKVEKLEESLE--KANVFKLSSEK--LQQENELMQQKIDLLEDRLQSSDEEL 376
Cdd:pfam07888 115 EEKDALLAQRAAHEARIRELEEDiKTLTQRVLERETELErmKERAKKAGAQRkeEEAERKQLQAKLQQTEEELRSLSKEF 194

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1731025460 377 QSYIKLYQE---SVKEFQDTLDTIKK----ASKKTATDEP 409
Cdd:pfam07888 195 QELRNSLAQrdtQVLQLQDTITTLTQklttAHRKEAENEA 234

rad50

TIGR00606

rad50; All proteins in this family for which functions are known are involvedin recombination, ...

110-416

9.93e-05

Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.58 E-value: 9.93e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  110 EGLNKGVQLEDLIGMIKSAEKNILLLN----QARVRALEDLEKILSEKEEL-QREINGLEMRLAETDTRIEVAAQEKVHV 184
Cdd:TIGR00606  259 HNLSKIMKLDNEIKALKSRKKQMEKDNseleLKMEKVFQGTDEQLNDLYHNhQRTVREKERELVDCQRELEKLNKERRLL 338

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  185 ELLEDQFEELQKQLNFSSGTVQSmNGNLNDIPIDSLTKELHLLKSE-----NIVLKNDIQTLKEELsnvknadqhlaflE 259
Cdd:TIGR00606  339 NQEKTELLVEQGRLQLQADRHQE-HIRARDSLIQSLATRLELDGFErgpfsERQIKNFHTLVIERQ-------------E 404

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  260 KERSVLESSLKDLESKLSTSQEDGSKLSDlnaECMDLRNRVEHLQVLLDKATKQADQAIRVLQQNQELQEKVEKLEESLE 339
Cdd:TIGR00606  405 DEAKTAAQLCADLQSKERLKQEQADEIRD---EKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELR 481

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  340 KA-------NVFKLSSEKLQQENELMQQKIDLLEdRLQSSDEELQSyIKLYQESVKEfqdtldTIKKASKKTATDEPVND 412
Cdd:TIGR00606  482 KAerelskaEKNSLTETLKKEVKSLQNEKADLDR-KLRKLDQEMEQ-LNHHTTTRTQ------MEMLTKDKMDKDEQIRK 553


                   ....
gi 1731025460  413 MPWE 416
Cdd:TIGR00606  554 IKSR 557

sbcc

TIGR00618

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

139-379

1.18e-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: 46.12 E-value: 1.18e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  139 RVRALEDLEKILSEKEELQREINGLEMRLAETDTRIEVAAQEKVHVELLEDQFEELQkqlNFSSGTVQSMNGNlNDIPID 218
Cdd:TIGR00618  668 RVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIE---NASSSLGSDLAAR-EDALNQ 743

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  219 SLTKELHLLK-----SENIVLKNDIQTLKEELSNVKNAD--QHLAFLEKERSVLESSLKDLESKLSTSQEDGskLSDLNA 291
Cdd:TIGR00618  744 SLKELMHQARtvlkaRTEAHFNNNEEVTAALQTGAELSHlaAEIQFFNRLREEDTHLLKTLEAEIGQEIPSD--EDILNL 821

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  292 ECMDLRNRVEHLQVLLDKATKQADQAIRVL-------QQNQELQEKVEKLEESLEKANVFKlsseklqqenelmQQKIDL 364
Cdd:TIGR00618  822 QCETLVQEEEQFLSRLEEKSATLGEITHQLlkyeecsKQLAQLTQEQAKIIQLSDKLNGIN-------------QIKIQF 888

                          250
                   ....*....|....*
gi 1731025460  365 LEDRLQSSDEELQSY 379
Cdd:TIGR00618  889 DGDALIKFLHEITLY 903

Smc

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

239-408

1.20e-04

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.08 E-value: 1.20e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 239 QTLKEELsnvKNADQHLAFLEKERsvLESSLKDLESKLSTSQEdgsKLSDLNAECMDLRNRVEHLQVLLDKATKQADQAi 318
Cdd:COG1196   216 RELKEEL---KELEAELLLLKLRE--LEAELEELEAELEELEA---ELEELEAELAELEAELEELRLELEELELELEEA- 286

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 319 rvLQQNQELQEKVEKLEESL----EKANVFKLSSEKLQQENELMQQKIDLLEDRLQSSDEELQSYIKLYQESVKEFQDTL 394
Cdd:COG1196   287 --QAEEYELLAELARLEQDIarleERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364

                         170
                  ....*....|....
gi 1731025460 395 DTIKKASKKTATDE 408
Cdd:COG1196   365 EALLEAEAELAEAE 378

PRK11281

mechanosensitive channel MscK;

217-406

1.52e-04

mechanosensitive channel MscK;

Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 45.67 E-value: 1.52e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  217 IDSLTKELHLL------KSENIVLKNDIQTLKEELSNVKNADQHL--AFLEKERSVLES-SLKDLESKLSTSQEDGSK-- 285
Cdd:PRK11281    62 QQDLEQTLALLdkidrqKEETEQLKQQLAQAPAKLRQAQAELEALkdDNDEETRETLSTlSLRQLESRLAQTLDQLQNaq 141

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  286 --LSDLNAECMDLRNRVEHLQVLLDKATKQADQAIRVLQQNQELQekvekleESLEKANVFKLSSEK--LQQENELMQQK 361
Cdd:PRK11281   142 ndLAEYNSQLVSLQTQPERAQAALYANSQRLQQIRNLLKGGKVGG-------KALRPSQRVLLQAEQalLNAQNDLQRKS 214

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1731025460  362 I---DLLEDRLQSSDEELQSYIKLYQESVKEFQDTLDTIK-KASKKTAT 406
Cdd:PRK11281   215 LegnTQLQDLLQKQRDYLTARIQRLEHQLQLLQEAINSKRlTLSEKTVQ 263

MscS_porin

pfam12795

Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...

238-385

1.53e-04

Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.

Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 44.21 E-value: 1.53e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 238 IQTLKEELSNVKNADQhlaflEKERSVLES-SLKDLESKLSTSQED----GSKLSDLNAECMDLRNRVEHLQVLLDKATK 312
Cdd:pfam12795  53 LRELRQELAALQAKAE-----AAPKEILASlSLEELEQRLLQTSAQlqelQNQLAQLNSQLIELQTRPERAQQQLSEARQ 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 313 QADQAIRVLQQNQELQEKVEKLEESLEKANVFKLSSE--KLQQE-------NELMQQKIDLLEDRLQssdeELQSYIKLY 383
Cdd:pfam12795 128 RLQQIRNRLNGPAPPGEPLSEAQRWALQAELAALKAQidMLEQEllsnnnrQDLLKARRDLLTLRIQ----RLEQQLQAL 203


                  ..
gi 1731025460 384 QE 385
Cdd:pfam12795 204 QE 205

GumC

COG3206

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

163-408

1.58e-04

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

Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 1.58e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 163 LEMRLAETDTRIEvaaqekvhveLLEDQFEELQKQLnfssgtvqsmngnlndipiDSLTKELHLLKSENIVLKNDIQTlK 242
Cdd:COG3206   166 LELRREEARKALE----------FLEEQLPELRKEL-------------------EEAEAALEEFRQKNGLVDLSEEA-K 215

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 243 EELSNVKNADQHLAFLEKERSVLESSLKDLESKLSTSQEDGSKLSDlNAECMDLRNRVEHLQVLLDKATKQ-ADQAIRVl 321
Cdd:COG3206   216 LLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQ-SPVIQQLRAQLAELEAELAELSARyTPNHPDV- 293

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 322 qqnQELQEKVEKLEESLEKANVFKLSS-----EKLQQENELMQQKIDLLEDRLQSSDEELQSYIKLYQEsVKEFQDTLDT 396
Cdd:COG3206   294 ---IALRAQIAALRAQLQQEAQRILASleaelEALQAREASLQAQLAQLEARLAELPELEAELRRLERE-VEVARELYES 369

                         250
                  ....*....|..
gi 1731025460 397 IKKASKKTATDE 408
Cdd:COG3206   370 LLQRLEEARLAE 381

COG4913

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

125-394

1.62e-04

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

Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 1.62e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  125 IKSAEKNILLLNQARVRALEDLEKILSEKEELQREINGLEMRLAETDTRIEVAAQEKvHVELLEDQFEELQKqlnfSSGT 204
Cdd:COG4913    612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAER-EIAELEAELERLDA----SSDD 686

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  205 VQSMNGNLNDI--PIDSLTKELHLLKSENIVLKNDIQTLKEELSNVKnaDQHLAFLEKERSVLESSLKDLESKLSTSQED 282
Cdd:COG4913    687 LAALEEQLEELeaELEELEEELDELKGEIGRLEKELEQAEEELDELQ--DRLEAAEDLARLELRALLEERFAAALGDAVE 764

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  283 GSKLSDLNAECMDLRNRVEHLQVLLDKATKQ------------------ADQAIRVLQQ--NQELQEKVEKLEESLEKAN 342
Cdd:COG4913    765 RELRENLEERIDALRARLNRAEEELERAMRAfnrewpaetadldadlesLPEYLALLDRleEDGLPEYEERFKELLNENS 844

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1731025460  343 VFKLS--SEKLQQENELMQQKIDLLEDRLQSSDEELQSYIKL-YQES----VKEFQDTL 394
Cdd:COG4913    845 IEFVAdlLSKLRRAIREIKERIDPLNDSLKRIPFGPGRYLRLeARPRpdpeVREFRQEL 903

F-BAR_PombeCdc15_like

cd07651

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Schizosaccharomyces pombe ...

226-390

1.63e-04

The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Schizosaccharomyces pombe Cdc15, and similar proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. This subfamily is composed of Schizosaccharomyces pombe Cdc15 and Imp2, and similar proteins. These proteins contain an N-terminal F-BAR domain and a C-terminal SH3 domain. S. pombe Cdc15 and Imp2 play both distinct and overlapping roles in the maintenance and strengthening of the contractile ring at the division site, which is required in cell division. Cdc15 is a component of the actomyosin ring and is required in normal cytokinesis. Imp2 colocalizes with the medial ring during septation and is required for normal septation. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.

Pssm-ID: 153335 [Multi-domain] Cd Length: 236 Bit Score: 44.22 E-value: 1.63e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 226 LLKSENIVLKNDIQTLKEELSNVknADQHLAFLEKERSVLESSLKDLESKLStsqedgsklsdlnaecmDLRNRVE-HLQ 304
Cdd:cd07651    50 LGGSEEGGLKNSLDTLRLETESM--AKSHLKFAKQIRQDLEEKLAAFASSYT-----------------QKRKKIQsHME 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 305 VLLDKatKQadqairvlQQNQELQEKVEKLEESLEKANVFKLSSEKLQ-QENELMQQKIDLLEDRLQSSDEELQSYIKLY 383
Cdd:cd07651   111 KLLKK--KQ--------DQEKYLEKAREKYEADCSKINSYTLQSQLTWgKELEKNNAKLNKAQSSINSSRRDYQNAVKAL 180


                  ....*..
gi 1731025460 384 QESVKEF 390
Cdd:cd07651   181 RELNEIW 187

sbcc

TIGR00618

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

137-360

1.93e-04

Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 45.34 E-value: 1.93e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  137 QARVRALEDLEKILSEKEELQREINGLEMRLAETDTRIEVA--AQEKVHVELLEDQFE----ELQKQLNFSSGTVQSMNG 210
Cdd:TIGR00618  253 EEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAplAAHIKAVTQIEQQAQrihtELQSKMRSRAKLLMKRAA 332

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  211 NLND-IPIDSLTKELHLLKSENIVLK--NDIQTL-KEELSNVKNADQHLAFLEKERSVLESSLKDLESKLSTSQEDGSKl 286
Cdd:TIGR00618  333 HVKQqSSIEEQRRLLQTLHSQEIHIRdaHEVATSiREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQAT- 411

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1731025460  287 sdlnAECMDLRNRVEHLQVLLDKATKQADQAIRVLQQ---NQELQEKVEKLEESLEKANVFKLSSEKLQQENELMQQ 360
Cdd:TIGR00618  412 ----IDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAaaiTCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQ 484

TPR_MLP1_2

pfam07926

TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...

151-276

1.96e-04

TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.

Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 42.24 E-value: 1.96e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 151 SEKEELQREINGLEMRLAETDTRIEVAAQEkvhvelLEDQFEELQK-QLNFSsgtvQSMNGNLNDIpidsltKELHLLKS 229
Cdd:pfam07926   1 AELSSLQSEIKRLKEEAADAEAQLQKLQED------LEKQAEIAREaQQNYE----RELVLHAEDI------KALQALRE 64

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1731025460 230 ENIVLKNDIQTLKEELSNVKNA-DQHLAFLEKERSVLESSLKDLESKL 276
Cdd:pfam07926  65 ELNELKAEIAELKAEAESAKAElEESEESWEEQKKELEKELSELEKRI 112

PLN03229

acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional

148-377

2.02e-04

acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional

Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 45.23 E-value: 2.02e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 148 KILSEK----EELQREINgleMRLAETDTRIEVaaQEKVHVELLEDQFEELQKQLNFSSGTVQSmngnlndipIDSLTKE 223
Cdd:PLN03229  547 KALSEKkskaEKLKAEIN---KKFKEVMDRPEI--KEKMEALKAEVASSGASSGDELDDDLKEK---------VEKMKKE 612

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 224 LHLlksenivlkndiqtlkeELSNV-KNADQHLAFLEKER--SVLESSLKDLESKL-STSQEDGSKLSDLnAECMDLRNR 299
Cdd:PLN03229  613 IEL-----------------ELAGVlKSMGLEVIGVTKKNkdTAEQTPPPNLQEKIeSLNEEINKKIERV-IRSSDLKSK 674

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1731025460 300 VEHLQVLLDKATKQADQAirvlqqnqeLQEKVEKLEESLEKANVFKLSSEKLQQENELMQQKIDLLEDRLQSSDEELQ 377
Cdd:PLN03229  675 IELLKLEVAKASKTPDVT---------EKEKIEALEQQIKQKIAEALNSSELKEKFEELEAELAAARETAAESNGSLK 743

PRK04778

septation ring formation regulator EzrA; Provisional

143-399

2.14e-04

septation ring formation regulator EzrA; Provisional

Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 45.21 E-value: 2.14e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 143 LEDLEKILSEKEEL---------QREINGLEMRLAETDTRI--------EVAAQEKVH---VELLEDQFEELQKQL---N 199
Cdd:PRK04778   81 LPDIEEQLFEAEELndkfrfrkaKHEINEIESLLDLIEEDIeqileelqELLESEEKNreeVEQLKDLYRELRKSLlanR 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 200 FSSGTVqsmngnlndipIDSLTKELHLLKSEnivlKNDIQTLKEELSNVKnADQHLAFLEKERSVLESSLKDLESKLSTS 279
Cdd:PRK04778  161 FSFGPA-----------LDELEKQLENLEEE----FSQFVELTESGDYVE-AREILDQLEEELAALEQIMEEIPELLKEL 224

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 280 QED-GSKLSDLNAECMDLRN---RVEHLQVL-----LDKATKQADQAIRVL------QQNQELQEKVEKLEESLE----- 339
Cdd:PRK04778  225 QTElPDQLQELKAGYRELVEegyHLDHLDIEkeiqdLKEQIDENLALLEELdldeaeEKNEEIQERIDQLYDILErevka 304

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1731025460 340 KANVFKLSS------EKLQQENELMQQKIDLLEDRLQSSDEELqsyiklyqESVKEFQDTLDTIKK 399
Cdd:PRK04778  305 RKYVEKNSDtlpdflEHAKEQNKELKEEIDRVKQSYTLNESEL--------ESVRQLEKQLESLEK 362

235kDa-fam

TIGR01612

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...

149-455

2.31e-04

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.

Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 45.43 E-value: 2.31e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  149 ILSEKEELQREINGLEMRLAETDTRI--EVAAQEKVHVELLEdqfEELQKQLNFSSGTVQSMNGNLNDIPIDSLTKElhl 226
Cdd:TIGR01612 1031 IEQKIEDANKNIPNIEIAIHTSIYNIidEIEKEIGKNIELLN---KEILEEAEINITNFNEIKEKLKHYNFDDFGKE--- 1104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  227 lksENIVLKNDIQTLKEELSNV-KNADQHLAFLEKERSVLESSLKDLESKLStSQEDGSKLSDLNAECMDLRNRVEHLQV 305
Cdd:TIGR01612 1105 ---ENIKYADEINKIKDDIKNLdQKIDHHIKALEEIKKKSENYIDEIKAQIN-DLEDVADKAISNDDPEEIEKKIENIVT 1180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  306 LLDKATKQADQAIRVLQQnqelQEKVEKLEESLEKANVFKLSSEklQQENELMQQKIDLLEDRLQSSDEELQSYIKlyqe 385
Cdd:TIGR01612 1181 KIDKKKNIYDEIKKLLNE----IAEIEKDKTSLEEVKGINLSYG--KNLGKLFLEKIDEEKKKSEHMIKAMEAYIE---- 1250

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  386 svkefqdTLDTIKKASKktatdEPVNDMPWEFWSRLLLLIDgwlleeKISGDDAKLLKEMAWKRDARIYD 455
Cdd:TIGR01612 1251 -------DLDEIKEKSP-----EIENEMGIEMDIKAEMETF------NISHDDDKDHHIISKKHDENISD 1302

ATG17_like

pfam04108

Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ...

258-414

2.44e-04

Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.

Pssm-ID: 427715 [Multi-domain] Cd Length: 360 Bit Score: 44.69 E-value: 2.44e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 258 LEKERSVLE---SSLKDLESKLSTSQEDGSKLSDLN---AECMD-LRNRVEHLQVLLDKATKQADQAIrvlqqnQELQEK 330
Cdd:pfam04108   2 LSSAQDLCRwanELLTDARSLLEELVVLLAKIAFLRrglSVQLAnLEKVREGLEKVLNELKKDFKQLL------KDLDAA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 331 VEKLEESLEKANVFKLSSEKLQQENE-------LMQQKIDLLEDRLQSSDEELQSYIKLYQESVKEFQDTLDTIKKA-SK 402
Cdd:pfam04108  76 LERLEETLDKLRNTPVEPALPPGEEKqktlldfIDEDSVEILRDALKELIDELQAAQESLDSDLKRFDDDLRDLQKElES 155

                         170
                  ....*....|..
gi 1731025460 403 KTATDEPVNDMP 414
Cdd:pfam04108 156 LSSPSESISLIP 167

Myosin_tail_1

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

118-403

2.63e-04

Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.17 E-value: 2.63e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  118 LEDLIGMIKSAeknilllNQARVRALEDLEKILSEKEELQREINglEMRLAetdtRIEVAAQEKvhvelledqfeELQKQ 197
Cdd:pfam01576  779 LKELEAQIDAA-------NKGREEAVKQLKKLQAQMKDLQRELE--EARAS----RDEILAQSK-----------ESEKK 834

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  198 LnfssgtvQSMNGNLNDIPIDSLTKELHllksenivlKNDIQTLKEELSN-VKNADQHLAFLEKERSVLESSLKDLESKL 276
Cdd:pfam01576  835 L-------KNLEAELLQLQEDLAASERA---------RRQAQQERDELADeIASGASGKSALQDEKRRLEARIAQLEEEL 898

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  277 STSQedgsklsdLNAECMDLRNRvehlqvlldKATKQADQAIRVLQQNQELQEKVEKLEESLEKANvfKLSSEKLQQENE 356
Cdd:pfam01576  899 EEEQ--------SNTELLNDRLR---------KSTLQVEQLTTELAAERSTSQKSESARQQLERQN--KELKAKLQEMEG 959

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1731025460  357 LMQQK----IDLLEDRLQSSDEELQsyiklyQESvKEFQDTLDTIKKASKK 403
Cdd:pfam01576  960 TVKSKfkssIAALEAKIAQLEEQLE------QES-RERQAANKLVRRTEKK 1003

SPEC

cd00176

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...

245-400

2.69e-04

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here

Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 43.20 E-value: 2.69e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 245 LSNVKNADQHLAFLEKERSVLESSLKDLES---KLSTSQEDGS-----KLSDLNAECMDLRNRVEHLQVLLDKATKQADQ 316
Cdd:cd00176    32 LESVEALLKKHEALEAELAAHEERVEALNElgeQLIEEGHPDAeeiqeRLEELNQRWEELRELAEERRQRLEEALDLQQF 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 317 AIRVLQQNQELQEKVEKLEESLEKANVFKLssEKLQQENELMQQKIDLLEDRLQSSDEELQSYIKLYQE-SVKEFQDTLD 395
Cdd:cd00176   112 FRDADDLEQWLEEKEAALASEDLGKDLESV--EELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPdADEEIEEKLE 189


                  ....*
gi 1731025460 396 TIKKA 400
Cdd:cd00176   190 ELNER 194

DUF3584

pfam12128

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...

117-471

2.75e-04

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: 44.83 E-value: 2.75e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  117 QLEDLIGMIKSAEKNILLLNQARVRALEDLEKILSEKEELQREIN-GLEMRLAETDTRI-EVAAQEKVHVELLEDQFEEL 194
Cdd:pfam12128  626 QLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNkALAERKDSANERLnSLEAQLKQLDKKHQAWLEEQ 705

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  195 QKQLNFSSgtvqsmngnlndipidslTKELHLLKSENIVLKNDIQTLKEELSNVK-NADQHLAFLEKERSvlesslKDLE 273
Cdd:pfam12128  706 KEQKREAR------------------TEKQAYWQVVEGALDAQLALLKAAIAARRsGAKAELKALETWYK------RDLA 761

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  274 SKlstsQEDGSKLSDLNAECMDLRNRVEHLQVLLDKATKQAD-QAIRVLQQNQELQEKVEKLEESLE--KANVFKLSSE- 349
Cdd:pfam12128  762 SL----GVDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDwYQETWLQRRPRLATQLSNIERAISelQQQLARLIADt 837

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  350 KLQQENELMQQK-IDLLEDRLQSS-------------------DEELQSYIKLYQESVKEFQDTLDTIKKASKKTaTDEP 409
Cdd:pfam12128  838 KLRRAKLEMERKaSEKQQVRLSENlrglrcemsklatlkedanSEQAQGSIGERLAQLEDLKLKRDYLSESVKKY-VEHF 916

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1731025460  410 VNDM-------PWEFWSRLLLLIDGWLLEEKISGDDAKLLKEMAWKRDARIYDAYMACKEKNELEAVAL 471
Cdd:pfam12128  917 KNVIadhsgsgLAETWESLREEDHYQNDKGIRLLDYRKLVPYLEQWFDVRVPQSIMVLREQVSILGVDL 985

PRK02224

DNA double-strand break repair Rad50 ATPase;

102-392

2.94e-04

DNA double-strand break repair Rad50 ATPase;

Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 2.94e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 102 EITGEVDTEGLNKGVQLEDLIGMIKSAEKNILLLNQARVRALEDLEKILSEKEELQREINGLEMRLAETDT-------RI 174
Cdd:PRK02224  363 EEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEAtlrtareRV 442

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 175 EVAAQ---------------EKVHVELLED---QFEELQKQLNFSSGTVQSMNGNLNDIpidsltKELHLLKSEnivlkn 236
Cdd:PRK02224  443 EEAEAlleagkcpecgqpveGSPHVETIEEdreRVEELEAELEDLEEEVEEVEERLERA------EDLVEAEDR------ 510

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 237 dIQTLKEELSNV-KNADQHLAFLEKERSVLESSLK---DLESKLSTSQEDGSK-----------LSDLN---AECMDLRN 298
Cdd:PRK02224  511 -IERLEERREDLeELIAERRETIEEKRERAEELREraaELEAEAEEKREAAAEaeeeaeeareeVAELNsklAELKERIE 589

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 299 RVEHLQVLLDKAT-----------KQADQAIRVLQQNQELQEKVEK---LEESLEKANVfklssEKLQQENELMQQKIDL 364
Cdd:PRK02224  590 SLERIRTLLAAIAdaedeierlreKREALAELNDERRERLAEKRERkreLEAEFDEARI-----EEAREDKERAEEYLEQ 664

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1731025460 365 LEDRLQSSDEE---LQSYIKLYQESVKEFQD 392
Cdd:PRK02224  665 VEEKLDELREErddLQAEIGAVENELEELEE 695

Lebercilin

pfam15619

Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...

238-378

3.09e-04

Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.

Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 42.97 E-value: 3.09e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 238 IQTLKEELSNvknADQHLAFLEKERSVLESSLKDLESKLSTSQEDGSKLSDL----NAECMDLRNRVEHLQ---VLLDKA 310
Cdd:pfam15619  13 IKELQNELAE---LQSKLEELRKENRLLKRLQKRQEKALGKYEGTESELPQLiarhNEEVRVLRERLRRLQekeRDLERK 89

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1731025460 311 TKQADQAIrvlqqnQELQEKVEKLEeslekanvfKLSSEKLQQENELMQQKIDLLEDRLQSSDEELQS 378
Cdd:pfam15619  90 LKEKEAEL------LRLRDQLKRLE---------KLSEDKNLAEREELQKKLEQLEAKLEDKDEKIQD 142

GT4_WfcD-like

cd03795

Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...

699-928

3.76e-04

Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP-linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria and eukaryotes.

Pssm-ID: 340826 [Multi-domain] Cd Length: 355 Bit Score: 43.80 E-value: 3.76e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 699 IVTTvSPTYAQEvrraegghglHSTLNFHSKKFFGILNGIDTDVWNPSTDSFIKVQYNandlqgkaenkdalrrhlglss 778
Cdd:cd03795   141 IIAT-SPNYVET----------SPTLREFKNKVRVIPLGIDKNVYNIPRVDFENIKRE---------------------- 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 779 NVRKPLVGCITRLVPQKGIH-LIRYAIYRTLELggqfVLLGSSPvphIQREFEDIAnHFQSHDQIRLV-LAYDESLSHWi 856
Cdd:cd03795   188 KKGKKIFLFIGRLVYYKGLDyLIEAAQYLNYPI----VIGGEGP---LKPDLEAQI-ELNLLDNVKFLgRVDDEEKVIY- 258

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1731025460 857 YAASDMFIIPSIF--EPCGLTQMIAMRYGsIPIVrkTGGLNDSVFDVDdettptelQNGYTFLT--P-DEQGLNNAL 928
Cdd:cd03795   259 LHLCDVFVFPSVLrsEAFGIVLLEAMMCG-KPVI--STNIGTGVPYVN--------NNGETGLVvpPkDPDALAEAI 324

YhaN

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

260-403

3.89e-04

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 3.89e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 260 KERSVLESSLKDLESKLSTSQEDGSKLSDLNAECMDLRNRVEHLQVLLDKATKQ---ADQAIRVLQQNQELQEKVEKLEE 336
Cdd:COG4717    71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLlqlLPLYQELEALEAELAELPERLEE 150

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1731025460 337 SLEKANVFK-LSSEKLQQENELMQQKIDL---LEDRLQSSDEELQSYIKLYQESVKEFQDTLDTIKKASKK 403
Cdd:COG4717   151 LEERLEELReLEEELEELEAELAELQEELeelLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEE 221

Filament

pfam00038

Intermediate filament protein;

139-398

4.12e-04

Intermediate filament protein;

Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 43.76 E-value: 4.12e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 139 RVRALE----DLEKILSEKEELQ-REINGL----EMRLAETDTRIEVAAQEKVHVEL----LEDQFEELQKQLNFSSGTV 205
Cdd:pfam00038  19 KVRFLEqqnkLLETKISELRQKKgAEPSRLyslyEKEIEDLRRQLDTLTVERARLQLeldnLRLAAEDFRQKYEDELNLR 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 206 QSMNGNLNDipidsLTKELHLLKSENIVLKNDIQTLKEElsnvknadqhLAFLekeRSVLESSLKDLESKLSTSQ----- 280
Cdd:pfam00038  99 TSAENDLVG-----LRKDLDEATLARVDLEAKIESLKEE----------LAFL---KKNHEEEVRELQAQVSDTQvnvem 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 281 EDGSKLsDLNAECMDLRNRVEhlqVLLDKATKQADQAIRvlQQNQELQEKVEKLEESL----EKANVFKLSSEKLQQENE 356
Cdd:pfam00038 161 DAARKL-DLTSALAEIRAQYE---EIAAKNREEAEEWYQ--SKLEELQQAAARNGDALrsakEEITELRRTIQSLEIELQ 234

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1731025460 357 LMQQKIDLLEDRLQSSDEELQSYIKLYQESVKEFQDTLDTIK 398
Cdd:pfam00038 235 SLKKQKASLERQLAETEERYELQLADYQELISELEAELQETR 276

DUF4686

pfam15742

Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ...

135-394

4.70e-04

Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.

Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 43.51 E-value: 4.70e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 135 LNQARVRaLEDLEKILS----EKEELQREINGLEMRLAETDTRI-------EVAAQEKVHVELLEDQFEELQKQLNfssg 203
Cdd:pfam15742  64 LKQAQQK-LLDSTKMCSsltaEWKHCQQKIRELELEVLKQAQSIksqnslqEKLAQEKSRVADAEEKILELQQKLE---- 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 204 tvQSMNGNLNDIPIdsLTKELhllksenivLKNDIQTLKEELSNVKnadQHLAFLEKERSVLESSLKDLESKLSTSQEDG 283
Cdd:pfam15742 139 --HAHKVCLTDTCI--LEKKQ---------LEERIKEASENEAKLK---QQYQEEQQKRKLLDQNVNELQQQVRSLQDKE 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 284 SKLSDLNAEcmdLRNRVEHLQVLLDKATKQADQAIRVLQQNQELQEKV-------EKLEESLEK------ANVFKLSSEK 350
Cdd:pfam15742 203 AQLEMTNSQ---QQLRIQQQEAQLKQLENEKRKSDEHLKSNQELSEKLsslqqekEALQEELQQvlkqldVHVRKYNEKH 279

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1731025460 351 LQQENELMQQKiDLLEDRLQSSDE---ELQSYIKLYQ---ESVKEFQDTL 394
Cdd:pfam15742 280 HHHKAKLRRAK-DRLVHEVEQRDErikQLENEIGILQqqsEKEKAFQKQV 328

SMC_N

pfam02463

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

227-471

5.77e-04

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

Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.81 E-value: 5.77e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  227 LKSENIVLKNDIQTLKEELSNVKNADQHLAFLEKERSVLESSLKDLESKLSTSQEDgsklsDLNAECMDLRNRVEHLQVL 306
Cdd:pfam02463  185 LAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERID-----LLQELLRDEQEEIESSKQE 259

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  307 LDKATKQADQairvLQQNQELQEKVEKLEEslEKANVFKLSSEKLQQENELMQQKIDLLEDRLQSSDEELQSYIKLYQES 386
Cdd:pfam02463  260 IEKEEEKLAQ----VLKENKEEEKEKKLQE--EELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKE 333

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  387 VKEFQDTLDTIKKASKKTATDEPVNDmpwefwsrLLLLIDGWLLEEKISGDDAKLLKEMAWKRDARIYDAYMACKEKNEL 466
Cdd:pfam02463  334 KEEIEELEKELKELEIKREAEEEEEE--------ELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEK 405


                   ....*
gi 1731025460  467 EAVAL 471
Cdd:pfam02463  406 EAQLL 410

GT4_ExpE7-like

cd03823

glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...

778-968

5.92e-04

glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ExpE7 in Sinorhizobium meliloti has been shown to be involved in the biosynthesis of galactoglucans (exopolysaccharide II).

Pssm-ID: 340850 [Multi-domain] Cd Length: 357 Bit Score: 43.09 E-value: 5.92e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 778 SNVRKPLVGCITRLVPQKGIHLIRYAIYRTLELGGQFVLLGSSPvphiqrefEDIANHFQSHDQIRLVLAYDESLSHWIY 857
Cdd:cd03823   187 PGTERLRFGYIGRLTEEKGIDLLVEAFKRLPREDIELVIAGHGP--------LSDERQIEGGRRIAFLGRVPTDDIKDFY 258

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 858 AASDMFIIPSIF-EPCGLTQMIAMRYGSIPIVRKTGGLNDSVFDVddettptelQNGYTFLTPDEQGLNNALERAfshyL 936
Cdd:cd03823   259 EKIDVLVVPSIWpEPFGLVVREAIAAGLPVIASDLGGIAELIQPG---------VNGLLFAPGDAEDLAAAMRRL----L 325

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1731025460 937 NNPSSWQQLVQKVMDVDFSwETSAAQYEELYS 968
Cdd:cd03823   326 TDPALLERLRAGAEPPRST-ESQAEEYLKLYR 356

PRK01156

chromosome segregation protein; Provisional

114-304

6.01e-04

chromosome segregation protein; Provisional

Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.74 E-value: 6.01e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 114 KGVQLEDLigmiksAEKNILLLNQARVRALEDLEKILSEKEELQREINGLEMRLAETDTRIE-VAAQEKVHVELLEDQFE 192
Cdd:PRK01156  556 KSLKLEDL------DSKRTSWLNALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPdDKSYIDKSIREIENEAN 629

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 193 ELQKQLNFSSGtvqsmngnlNDIPIDSLTKELHLLKSENIVLKNDIQTLKEELSNVKNADQHLAFLEKERSVLESSLKDL 272
Cdd:PRK01156  630 NLNNKYNEIQE---------NKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARL 700

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1731025460 273 ESKLSTSQEDGSKLSDLNAecmDLRNRVEHLQ 304
Cdd:PRK01156  701 ESTIEILRTRINELSDRIN---DINETLESMK 729

DR0291

COG1579

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

252-400

6.04e-04

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

Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.60 E-value: 6.04e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 252 DQHLAFLEKERSVLESSLKDLESKLSTsqedgsklsdLNAECMDLRNRVEHLQvlldKATKQADQAIrvlqqnQELQEKV 331
Cdd:COG1579    16 DSELDRLEHRLKELPAELAELEDELAA----------LEARLEAAKTELEDLE----KEIKRLELEI------EEVEARI 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1731025460 332 EKLEESLEKAnvfklSSEK----LQQENELMQQKIDLLEDRLQSSD---EELQSYIKLYQESVKEFQDTLDTIKKA 400
Cdd:COG1579    76 KKYEEQLGNV-----RNNKeyeaLQKEIESLKRRISDLEDEILELMeriEELEEELAELEAELAELEAELEEKKAE 146

PLN03229

acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional

143-396

6.61e-04

acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional

Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 43.69 E-value: 6.61e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 143 LEDL-EKILSEKEELQREIN-GLEMRLAETDTRIEVAAQEKVHVELLEDQFEELQKQLNFSSGTVQSMNGNLNDiPIDSL 220
Cdd:PLN03229  438 VEKLkEQILKAKESSSKPSElALNEMIEKLKKEIDLEYTEAVIAMGLQERLENLREEFSKANSQDQLMHPVLME-KIEKL 516

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 221 TKELHLLKSEN---IVLKNDIQTLKEelsnvknadqhlafLEKERSVLESSLKDLESKLSTSQedgsKLSdlnaECMDLR 297
Cdd:PLN03229  517 KDEFNKRLSRApnyLSLKYKLDMLNE--------------FSRAKALSEKKSKAEKLKAEINK----KFK----EVMDRP 574

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 298 NRVEHLQVLLDKATKQADQAIRVLqqNQELQEKVEKL--EESLEKANVFKlsSEKLQQENeLMQQKIDLLEdrlQSSDEE 375
Cdd:PLN03229  575 EIKEKMEALKAEVASSGASSGDEL--DDDLKEKVEKMkkEIELELAGVLK--SMGLEVIG-VTKKNKDTAE---QTPPPN 646

                         250       260
                  ....*....|....*....|..
gi 1731025460 376 LQSYI-KLYQESVKEFQDTLDT 396
Cdd:PLN03229  647 LQEKIeSLNEEINKKIERVIRS 668

TelA

pfam05816

Toxic anion resistance protein (TelA); This family consists of several prokaryotic TelA like ...

206-332

7.81e-04

Toxic anion resistance protein (TelA); This family consists of several prokaryotic TelA like proteins. TelA and KlA are associated with tellurite resistance and plasmid fertility inhibition.

Pssm-ID: 461748 Cd Length: 330 Bit Score: 42.89 E-value: 7.81e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 206 QSMNGNLNDIPIDsltkelhlLKSENIVLKNDIQTLKEELSNVKNADQHL--------AFLEKERSVLESSLKDLESKlS 277
Cdd:pfam05816  91 QTAGAQIDKIVVE--------LEKGQDELLKDNAMLDQMYEKNLEYFKELekyiaageLKLEELDAELLPELEAKAAA-S 161

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1731025460 278 TSQEDGSKLSDLNAECMDLRNRVEHLQVLLDKATKQADQaIRVLQQ-NQELQEKVE 332
Cdd:pfam05816 162 GDPEDAQALRDLRQALFRLEQRIHDLELQRAVSIQTAPQ-IRLVQNnNQELIEKIQ 216

COG5022

Myosin heavy chain [General function prediction only];

117-412

7.89e-04

Myosin heavy chain [General function prediction only];

Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 43.53 E-value: 7.89e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  117 QLEDLIGMIKSAEknillLNQARVRALEDLEKILSEKEElqreinglemrlaetdtriEVAAQEKVHVELLEDQFEELQK 196
Cdd:COG5022    834 ETEEVEFSLKAEV-----LIQKFGRSLKAKKRFSLLKKE-------------------TIYLQSAQRVELAERQLQELKI 889

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  197 QlnfssgtvqsmNGNLNDIPIDSLTKElhllkSENIVLKNDIQTLKEELSNVKNadQHLAFLEK---ERSVLESSLKDLE 273
Cdd:COG5022    890 D-----------VKSISSLKLVNLELE-----SEIIELKKSLSSDLIENLEFKT--ELIARLKKllnNIDLEEGPSIEYV 951

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  274 SK--LSTSQEDGSKLSDLNAECMDLRNRVEHLQVLLDKATKQADQAIRVLQ----QNQELQEKVEKLEE----SLEKANV 343
Cdd:COG5022    952 KLpeLNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAelskQYGALQESTKQLKElpveVAELQSA 1031

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1731025460  344 FKL---SSEKLQQENELMQQKIDLLED--RLQSSDEELQSYIKLYQESVKEFQDTLDTIKKASKKTATDEPVND 412
Cdd:COG5022   1032 SKIissESTELSILKPLQKLKGLLLLEnnQLQARYKALKLRRENSLLDDKQLYQLESTENLLKTINVKDLEVTN 1105

PTZ00121

MAEBL; Provisional

141-403

9.79e-04

MAEBL; Provisional

Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 9.79e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  141 RALEDLEKILSEK--EELQReinGLEMRLAETDTRIEVAAQEKVHVELLEDQFEELQKQLNFSSGTVQSMNGNLNDIPID 218
Cdd:PTZ00121  1534 KKADEAKKAEEKKkaDELKK---AEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE 1610

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  219 SLTKE------LHLLKSENIVLKNDIQTLKEELSNVKNADQhLAFLEKERSVLESSLKDLESK-------LSTSQEDGSK 285
Cdd:PTZ00121  1611 EAKKAeeakikAEELKKAEEEKKKVEQLKKKEAEEKKKAEE-LKKAEEENKIKAAEEAKKAEEdkkkaeeAKKAEEDEKK 1689

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  286 LSDLNAECMDLRNRVEHLQVLLDKATKQADQ--------AIRVLQQNQELQEKVEKLEESL----EKANVFKLSSEKLQQ 353
Cdd:PTZ00121  1690 AAEALKKEAEEAKKAEELKKKEAEEKKKAEElkkaeeenKIKAEEAKKEAEEDKKKAEEAKkdeeEKKKIAHLKKEEEKK 1769

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1731025460  354 ENELMQQKIDLLEDRLQSSDEELQSYIklyQESVKEFQDTLDTIKKASKK 403
Cdd:PTZ00121  1770 AEEIRKEKEAVIEEELDEEDEKRRMEV---DKKIKDIFDNFANIIEGGKE 1816

Myosin_tail_1

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

237-413

1.11e-03

Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.85 E-value: 1.11e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  237 DIQTLKEELSNVKNADQHLaflekersvlESSLKDLESKLSTSQEDGSKLSD-LNAEcMDLRNRVEHLQVlldkatkqad 315
Cdd:pfam01576    6 EMQAKEEELQKVKERQQKA----------ESELKELEKKHQQLCEEKNALQEqLQAE-TELCAEAEEMRA---------- 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  316 qaiRVLQQNQELQEKVEKLEESLEKAnvfKLSSEKLQQENELMQQKIDLLEDRLqssDEELQSYIKLYQESV------KE 389
Cdd:pfam01576   65 ---RLAARKQELEEILHELESRLEEE---EERSQQLQNEKKKMQQHIQDLEEQL---DEEEAARQKLQLEKVtteakiKK 135

                          170       180
                   ....*....|....*....|....*....
gi 1731025460  390 FQDTL----DTIKKASK-KTATDEPVNDM 413
Cdd:pfam01576  136 LEEDIllleDQNSKLSKeRKLLEERISEF 164

ZapB

COG3074

Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome ...

312-371

1.28e-03

Cell division protein ZapB, interacts with FtsZ [Cell cycle control, cell division, chromosome partitioning];

Pssm-ID: 442308 [Multi-domain] Cd Length: 79 Bit Score: 38.41 E-value: 1.28e-03

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1731025460 312 KQADQAIRVLQQ-NQELQEKVEKLEESLEKAnvfKLSSEKLQQENELMQQKIDLLEDRLQS 371
Cdd:COG3074    14 QQAVDTIELLQMeVEELKEKNEELEQENEEL---QSENEELQSENEQLKTENAEWQERIRS 71

GT4_UGDG-like

cd03817

UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...

751-930

1.28e-03

UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. UDP-glucose-diacylglycerol glucosyltransferase (EC 2.4.1.337, UGDG; also known as 1,2-diacylglycerol 3-glucosyltransferase) catalyzes the transfer of glucose from UDP-glucose to 1,2-diacylglycerol forming 3-D-glucosyl-1,2-diacylglycerol.

Pssm-ID: 340844 [Multi-domain] Cd Length: 372 Bit Score: 42.27 E-value: 1.28e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 751 IKVQYNANDLQG-KAENKDALRRHLGLSSnvRKPLVGCITRLVPQKGIHLIRYAIYRTLELGG-QFVLLGSSPVPHiqrE 828
Cdd:cd03817   171 IEVIPNGIDLDKfEKPLNTEERRKLGLPP--DEPILLYVGRLAKEKNIDFLLRAFAELKKEPNiKLVIVGDGPERE---E 245

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 829 FEDIANHFQSHDQIRLV--LAYDEsLSHwIYAASDMFIIPSIFEPCGLTQMIAMRYGsIPIV-RKTGGLNDSVFDVDdet 905
Cdd:cd03817   246 LKELARELGLADKVIFTgfVPREE-LPE-YYKAADLFVFASTTETQGLVYLEAMAAG-LPVVaAKDPAASELVEDGE--- 319

                         170       180
                  ....*....|....*....|....*
gi 1731025460 906 tptelqNGYTFlTPDEQGLNNALER 930
Cdd:cd03817   320 ------NGFLF-EPNDETLAEKLLH 337

HlpA

COG2825

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

309-408

1.31e-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: 40.59 E-value: 1.31e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 309 KATKQADQAIRVL-----QQNQELQEKVEKLEESLEKANVFKLSSEKLQQENELMQQKIDLLEDRlQSSDEELQsyikly 383
Cdd:COG2825    39 PEGKAAQKKLEKEfkkrqAELQKLEKELQALQEKLQKEAATLSEEERQKKERELQKKQQELQRKQ-QEAQQDLQ------ 111

                          90       100
                  ....*....|....*....|....*
gi 1731025460 384 QESVKEFQDTLDTIKKASKKTATDE 408
Cdd:COG2825   112 KRQQELLQPILEKIQKAIKEVAKEE 136

OmpH

smart00935

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

322-408

1.51e-03

Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 39.87 E-value: 1.51e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  322 QQNQELQEKVEKLEESLEKANVFKLSSEKLQQENELMQQKIDLLEDRlQSSDEELQsyiklyQESVKEFQDTLDTIKKAS 401
Cdd:smart00935  32 AELEKLEKELQKLKEKLQKDAATLSEAAREKKEKELQKKVQEFQRKQ-QKLQQDLQ------KRQQEELQKILDKINKAI 104


                   ....*..
gi 1731025460  402 KKTATDE 408
Cdd:smart00935 105 KEVAKKK 111

GT4_WavL-like

cd03819

Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...

582-898

1.93e-03

Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 family of glycosyltransferases. WavL in Vibrio cholerae has been shown to be involved in the biosynthesis of the lipopolysaccharide core.

Pssm-ID: 340846 [Multi-domain] Cd Length: 345 Bit Score: 41.57 E-value: 1.93e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 582 RAQYYGEHDDFKRFSYFSRA----ALELLLRAgKRPDIIHCHdwqTAFIAPLYWDLyypKGLNSARICFTCHN---FEYQ 654
Cdd:cd03819    43 RLRQIGIGLPGLKVPLLRALlgnvRLARLIRR-ERIDLIHAH---SRAPAWLGWLA---SRLTGVPLVTTVHGsylATYH 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 655 GTAPAsdlascgldvdqlnrqdrlqdnssHERINPVKGAVVFSNIV--TTVSPTYAQEVRraegghgLHStlnfhskkff 732
Cdd:cd03819   116 PKDFA------------------------LAVRARGDRVIAVSELVrdHLIEALGVDPER-------IRV---------- 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 733 gILNGIDTDVWNPstdsfikvqynandlqgkaENKDALRRHLGLSSNvrKPLVGCITRLVPQKGIHLIRYAIYRtLELGG 812
Cdd:cd03819   155 -IPNGVDTDRFPP-------------------EAEAEERAQLGLPEG--KPVVGYVGRLSPEKGWLLLVDAAAE-LKDEP 211

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 813 QFVLL--GSSPV-PHIQREFED--IANHFQSHDQIRLVLAYdeslshwiYAASDMFIIPSIFEPCGLTQMIAMRYGSIPI 887
Cdd:cd03819   212 DFRLLvaGDGPErDEIRRLVERlgLRDRVTFTGFREDVPAA--------LAASDVVVLPSLHEEFGRVALEAMACGTPVV 283

                         330
                  ....*....|.
gi 1731025460 888 VRKTGGLNDSV 898
Cdd:cd03819   284 ATDVGGAREIV 294

Smc

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

273-389

2.04e-03

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.23 E-value: 2.04e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 273 ESKLSTSQEDGSKLSDLNAEcmdLRNRVEHLQvlldkatKQADQA---------IRVLQQN------QELQEKVEKLEES 337
Cdd:COG1196   178 ERKLEATEENLERLEDILGE---LERQLEPLE-------RQAEKAeryrelkeeLKELEAEllllklRELEAELEELEAE 247

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1731025460 338 LEKAnvfKLSSEKLQQENELMQQKIDLLEDRLQSSDEELQSYIKLYQESVKE 389
Cdd:COG1196   248 LEEL---EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE 296

Filament

pfam00038

Intermediate filament protein;

235-391

2.11e-03

Intermediate filament protein;

Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 41.44 E-value: 2.11e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 235 KNDIQTLKEELSNvknadqhlaFLEKERSvLESSLKDLESKLSTSQEDG----SKLSDL-NAECMDLRNRVEHLQVllDK 309
Cdd:pfam00038   3 KEQLQELNDRLAS---------YIDKVRF-LEQQNKLLETKISELRQKKgaepSRLYSLyEKEIEDLRRQLDTLTV--ER 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 310 AtkqadqaiRVLQQNQELQEKVEKLEESLEKAnvfklSSEKLQQENELMQQKIDL---------LEDRLQSSDEELQSYI 380
Cdd:pfam00038  71 A--------RLQLELDNLRLAAEDFRQKYEDE-----LNLRTSAENDLVGLRKDLdeatlarvdLEAKIESLKEELAFLK 137

                         170
                  ....*....|.
gi 1731025460 381 KLYQESVKEFQ 391
Cdd:pfam00038 138 KNHEEEVRELQ 148

HMMR_N

pfam15905

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...

233-413

2.48e-03

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.

Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 41.34 E-value: 2.48e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 233 VLKNDIQTLKEELSNVKNADQHLAFLEKERSVLESSLKDL-------ESKLSTS-------------------------- 279
Cdd:pfam15905  60 ELKKKSQKNLKESKDQKELEKEIRALVQERGEQDKRLQALeeelekvEAKLNAAvrektslsasvaslekqlleltrvne 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 280 ------QEDGS--KLSDLNAECMDLRNRVEhlqvlldkaTKQadQAIRVLQQNQE--LQEKVEKLEESleKANVFKLSSE 349
Cdd:pfam15905 140 llkakfSEDGTqkKMSSLSMELMKLRNKLE---------AKM--KEVMAKQEGMEgkLQVTQKNLEHS--KGKVAQLEEK 206

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1731025460 350 KLQQENELMQQKID---LLE--DRLQSSDEELQSY---IKLYQESVKEFQDTLDTIKKA--SKKTATDEPVNDM 413
Cdd:pfam15905 207 LVSTEKEKIEEKSEtekLLEyiTELSCVSEQVEKYkldIAQLEELLKEKNDEIESLKQSleEKEQELSKQIKDL 280

Cast

pfam10174

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...

139-404

2.62e-03

Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 41.73 E-value: 2.62e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 139 RVRaLEDLEKILSEK-EELQR----------EINGLEMRLAETDTRIEVAaQEKVhvELLEDQFEELQKQLNFSSGTVQS 207
Cdd:pfam10174 351 RLR-LEEKESFLNKKtKQLQDlteekstlagEIRDLKDMLDVKERKINVL-QKKI--ENLQEQLRDKDKQLAGLKERVKS 426

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 208 MNGNLNDIPIDSLTKELHLLKSENIV-------------LKNDIQTLKEELsnvKNADQHLAFLEKERSVLESSLKDLES 274
Cdd:pfam10174 427 LQTDSSNTDTALTTLEEALSEKERIIerlkeqreredreRLEELESLKKEN---KDLKEKVSALQPELTEKESSLIDLKE 503

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 275 KLSTSQEDG----SKLSDLNAECMDLRNRVEHLQVLLDKATKQADQAirvlQQNQELQEKVEKLEeslEKANVFKLSSEK 350
Cdd:pfam10174 504 HASSLASSGlkkdSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAV----RTNPEINDRIRLLE---QEVARYKEESGK 576

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1731025460 351 LQQENELMQQKIDLLEDRLQSSDEELQSYIKLYQESVKEfqdtlDTIKKASKKT 404
Cdd:pfam10174 577 AQAEVERLLGILREVENEKNDKDKKIAELESLTLRQMKE-----QNKKVANIKH 625

PRK05771

V-type ATP synthase subunit I; Validated

120-307

2.69e-03

V-type ATP synthase subunit I; Validated

Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.45 E-value: 2.69e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 120 DLIGMIKSAEKNIL-LLNQARVRALEDLEKILSEK-EELQREINGLEMRLAETDTRIEVAAQEKVHVELLEDQFEELQKQ 197
Cdd:PRK05771   60 DKLRSYLPKLNPLReEKKKVSVKSLEELIKDVEEElEKIEKEIKELEEEISELENEIKELEQEIERLEPWGNFDLDLSLL 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 198 LNFSS-----GTVQSmNGNLNDIPIDSLTKELHLLKSEN------IVLKNDIQTLKEEL----------SNVKNADQHLA 256
Cdd:PRK05771  140 LGFKYvsvfvGTVPE-DKLEELKLESDVENVEYISTDKGyvyvvvVVLKELSDEVEEELkklgferlelEEEGTPSELIR 218

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1731025460 257 FLEKERSVLESSLKDLESKLSTSQEdgsKLSDLNAECMD-LRNRVEHLQVLL 307
Cdd:PRK05771  219 EIKEELEEIEKERESLLEELKELAK---KYLEELLALYEyLEIELERAEALS 267

Spc7

smart00787

Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...

135-399

2.87e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.

Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 40.77 E-value: 2.87e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  135 LNQARVRALEDLEKILSEKEELQREINglemRLAETDTRIE--VAAQeKVHVELLE-DQF--EELQKQLNFSSGTVQSMN 209
Cdd:smart00787  16 LNMTGIRFMELLTTKRRHTPAPAISLN----RISEEDCSLDqyVVAG-YCTVPLLElYQFscKELKKYISEGRDLFKEIE 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  210 GN-LNDIPIdsLTKElHLLKSENIvlkndIQTLKEELSNVKnadQHLAFLEKE-----RSVLESSLKD-LESKLSTSQED 282
Cdd:smart00787  91 EEtLINNPP--LFKE-YFSASPDV-----KLLMDKQFQLVK---TFARLEAKKmwyewRMKLLEGLKEgLDENLEGLKED 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  283 GSKLSDlnaecmdlrnRVEHLQVLLDKATKQADQAIRVLQQNQELQEKVEKLEESLEKANVFKLSseKLQQENELMQQKI 362
Cdd:smart00787 160 YKLLMK----------ELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRAKEKLK--KLLQEIMIKVKKL 227

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1731025460  363 DLLEDRLQSSDEELQSY---IKLYQESVKEFQDTLDTIKK 399
Cdd:smart00787 228 EELEEELQELESKIEDLtnkKSELNTEIAEAEKKLEQCRG 267

COG4913

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

250-397

3.09e-03

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

Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 3.09e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  250 NADQhLAFLEKERSVLESSLKDLESKLStsqedgsklsDLNAECMDLRNRVEHLQVLLDkatkQADQAIRVLQQNQELQE 329
Cdd:COG4913    608 NRAK-LAALEAELAELEEELAEAEERLE----------ALEAELDALQERREALQRLAE----YSWDEIDVASAEREIAE 672

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1731025460  330 KVEKLEEsLEKANVfKLssEKLQQENELMQQKIDLLEDRLQSSDEE---LQSYIKLYQESVKEFQDTLDTI 397
Cdd:COG4913    673 LEAELER-LDASSD-DL--AALEEQLEELEAELEELEEELDELKGEigrLEKELEQAEEELDELQDRLEAA 739

HAUS4

pfam14735

HAUS augmin-like complex subunit 4; This family includes HAUS augmin-like complex subunit 4. ...

226-363

3.13e-03

HAUS augmin-like complex subunit 4; This family includes HAUS augmin-like complex subunit 4. The HAUS augmin-like complex contributes to mitotic spindle assembly, maintenance of chromosome integrity and completion of cytokinesis.

Pssm-ID: 464287 Cd Length: 235 Bit Score: 40.32 E-value: 3.13e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 226 LLKSENIVLKNDIQTLKEE--LSNVKNAdQHLAFLEKERSVLESSLKDLESKlSTSQEDGSKLSDLNAEC--MDLRNRVE 301
Cdd:pfam14735  80 LLESEKRRLESEKEKLRENlvLLQRQFA-EYYQVLLQCLQLLQRLVLDHRLK-HQSDLDRKKKEYLEAKCeaMNLKLRVL 157

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 302 HLQVLLDKATKQADQAIRVLQqnQELQEKVEKLEESLEKAnVFKLSS--------EKLQQENELMQQKID 363
Cdd:pfam14735 158 ELELLLDTYTPETVPALRKIR--DYLEEALEEEEQELQKA-RLRLRSyeilgpdfEELVREYHRLRQEIE 224

Myosin_tail_1

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

139-403

3.90e-03

Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.31 E-value: 3.90e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  139 RVRALED----LEKILSEKEE----LQREINGLEMRLAETDTRIEvaaQEKVHVELLEDQFEELQKQLNfssGTVQSMNG 210
Cdd:pfam01576  490 RLRQLEDernsLQEQLEEEEEakrnVERQLSTLQAQLSDMKKKLE---EDAGTLEALEEGKKRLQRELE---ALTQQLEE 563

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  211 NlnDIPIDSLTKELHLLKSENIVLKNDIQTLKEELSNV----KNADQHLAfLEK--------ERSVLESSLKDLESK-LS 277
Cdd:pfam01576  564 K--AAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLekkqKKFDQMLA-EEKaisaryaeERDRAEAEAREKETRaLS 640

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  278 TS---QEDGSKLSDLNAECMDLRNRVEHLQVLLDKATKQA---DQAIRVL-QQNQELQEKVEKLEESLEKANVFKLSSEK 350
Cdd:pfam01576  641 LAralEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVhelERSKRALeQQVEEMKTQLEELEDELQATEDAKLRLEV 720

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1731025460  351 lqqeneLMQQKIDLLEDRLQSSDEELQSYIKLYQESVKEFQDTLDTIKK------ASKK 403
Cdd:pfam01576  721 ------NMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKqraqavAAKK 773

PTZ00464

SNF-7-like protein; Provisional

268-402

4.36e-03

SNF-7-like protein; Provisional

Pssm-ID: 240425 [Multi-domain] Cd Length: 211 Bit Score: 39.80 E-value: 4.36e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 268 SLKDLESKLSTSQED-GSKLSDLNAECMDLRNRVEHLQVLLDKATKQadQAIRVLQQNQELQekvekleeslekanvfkl 346
Cdd:PTZ00464   15 TLEDASKRIGGRSEVvDARINKIDAELMKLKEQIQRTRGMTQSRHKQ--RAMQLLQQKRMYQ------------------ 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1731025460 347 sseklQQENELMQQKIDLledrlqssdEELQSYIklyqESVKEFQDTLDTIKKASK 402
Cdd:PTZ00464   75 -----NQQDMMMQQQFNM---------DQLQFTT----ESVKDTKVQVDAMKQAAK 112

CENP-F_leu_zip

pfam10473

Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ...

205-329

4.72e-03

Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.

Pssm-ID: 463102 [Multi-domain] Cd Length: 140 Bit Score: 38.43 E-value: 4.72e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 205 VQSMNGNLNDiPIDSLTKELHLLKSENIVLKNDIQTLKEELSNVK----NADQHLAFLEKERSVLESSLKDLESKLSTSQ 280
Cdd:pfam10473  15 SERKADSLKD-KVENLERELEMSEENQELAILEAENSKAEVETLKaeieEMAQNLRDLELDLVTLRSEKENLTKELQKKQ 93

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1731025460 281 EdgsKLSDLNAECMDLRNRVEHLQVLLDKATKQADQAIRVLQ-QNQELQE 329
Cdd:pfam10473  94 E---RVSELESLNSSLENLLEEKEQEKVQMKEESKTAVEMLQtQLKELNE 140

GT4_WbdM_like

cd04951

LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ...

735-903

5.15e-03

LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases and is named after WbdM in Escherichia coli. In general glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found in bacteria.

Pssm-ID: 340857 [Multi-domain] Cd Length: 360 Bit Score: 40.12 E-value: 5.15e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 735 LNGIDTDVWNPSTDSFIKVQ----------YNANDL---QGKAENKDALRRHLGLSSNvrKPLVGCITRLVPQKGIHLIR 801
Cdd:cd04951   130 LCDITTNVSREALDEFIAKKafsknksvpvYNGIDLnkfKKDINVRLKIRNKLNLKND--EFVILNVGRLTEAKDYPNLL 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 802 YAIYRTLELGGQFVLL--GSSPvphIQREFEDIANHFQSHDQIRLVLAYDESLSHwiYAASDMFIIPSIFEPCGLTQMIA 879
Cdd:cd04951   208 LAISELILSKNDFKLLiaGDGP---LRNELERLICNLNLVDRVILLGQISNISEY--YNAADLFVLSSEWEGFGLVVAEA 282

                         170       180
                  ....*....|....*....|....
gi 1731025460 880 MRYGSIPIVRKTGGLNDSVFDVDD 903
Cdd:cd04951   283 MACERPVVATDAGGVAEVVGDHNY 306

YhaN

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

137-342

5.34e-03

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 5.34e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 137 QARVRALEDLEKILSEKEELQREINGLEMRLAETDTRIEVAAQEKVHVELLEDQFEELQKQLnfssgtvqsmngnlndip 216
Cdd:COG4717   350 QELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQL------------------ 411

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 217 idsltkELHLLKSENIVLKNDIQTLKEELSNVKnadQHLAFLEKERSVLESSLKDLESKLSTSQEDGSkLSDLNAECMDL 296
Cdd:COG4717   412 ------EELLGELEELLEALDEEELEEELEELE---EELEELEEELEELREELAELEAELEQLEEDGE-LAELLQELEEL 481

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1731025460 297 RNRVEHLqvLLDKATKQAdqAIRVLQQNQELQEKvEKLEESLEKAN 342
Cdd:COG4717   482 KAELREL--AEEWAALKL--ALELLEEAREEYRE-ERLPPVLERAS 522

PTZ00440

reticulocyte binding protein 2-like protein; Provisional

144-368

5.56e-03

reticulocyte binding protein 2-like protein; Provisional

Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 40.97 E-value: 5.56e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  144 EDLEKILSEKEELQREINGLEMRLAETDTRIEVAAQ------EKVHVELLEDQFEELQKQLNFSSGTVQSMNGNLNDIP- 216
Cdd:PTZ00440   805 ENKKNNQDLLNSYNILIQKLEAHTEKNDEELKQLLQkfptedENLNLKELEKEFNENNQIVDNIIKDIENMNKNINIIKt 884

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  217 -------------------------IDSLTKELHLLKSENIVLKND----IQTLKEELSNVKN--ADQHLAFLEKERSVL 265
Cdd:PTZ00440   885 lniainrsnsnkqlvehllnnkidlKNKLEQHMKIINTDNIIQKNEklnlLNNLNKEKEKIEKqlSDTKINNLKMQIEKT 964

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  266 ESSLKdlESKLSTSQEDGSKLSDLNA---ECMDLRNRVEHLQV---LLDKAT-----KQADQAI-----RVLQQNQELQE 329
Cdd:PTZ00440   965 LEYYD--KSKENINGNDGTHLEKLDKekdEWEHFKSEIDKLNVnynILNKKIddlikKQHDDIIelidkLIKEKGKEIEE 1042

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1731025460  330 KVEK----LEESLEKANVFKLSSEKLQQENELMQQKIDLLEDR 368
Cdd:PTZ00440  1043 KVDQyislLEKMKTKLSSFHFNIDIKKYKNPKIKEEIKLLEEK 1085

Mplasa_alph_rch

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...

113-403

5.56e-03

Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.77 E-value: 5.56e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 113 NKGVQLEDLIGMIKSAEKNILLLNQARVRALEDLEKILSEKEELQREINGLEMRLAETDTRIEvaaqekvhVELLEDQFE 192
Cdd:TIGR04523 493 SKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELK--------KENLEKEID 564

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 193 ELQKQlnfssgtvqsmngnlndipIDSLTKELHLLKSENIVLKNDIQTLKEELSNVKnadqhlafleKERSVLESSLKDL 272
Cdd:TIGR04523 565 EKNKE-------------------IEELKQTQKSLKKKQEEKQELIDQKEKEKKDLI----------KEIEEKEKKISSL 615

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 273 ESKLSTSQEDGSKLSdlnAECMDLRNRVEHLQVLLDKATKQADQAI----RVLQQNQELQEKVEKLEESLEKANVFKLSS 348
Cdd:TIGR04523 616 EKELEKAKKENEKLS---SIIKNIKSKKNKLKQEVKQIKETIKEIRnkwpEIIKKIKESKTKIDDIIELMKDWLKELSLH 692

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1731025460 349 EKLQQENELMQQKIDLLEDRLQSSDEELQsyiklyqeSVKEFQDTLDT-IKKASKK 403
Cdd:TIGR04523 693 YKKYITRMIRIKDLPKLEEKYKEIEKELK--------KLDEFSKELENiIKNFNKK 740

COG6

smart01087

Conserved oligomeric complex COG6; COG6 is a component of the conserved oligomeric golgi ...

181-397

5.60e-03

Conserved oligomeric complex COG6; COG6 is a component of the conserved oligomeric golgi complex, which is composed of eight different subunits and is required for normal golgi morphology and localisation.

Pssm-ID: 215018 Cd Length: 598 Bit Score: 40.38 E-value: 5.60e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  181 KVHVELLEDqFEELQKQLNFSSGTVQSMNGNlndipIDSLTKELHLLKSENIVLKNDIQTLKEELSNVKNADQHL-AFLE 259
Cdd:smart01087  18 KINGEFLSE-FKPVAEQLQRLSEDVQKLNNS-----CDSMKDQLNTAKNQTQDLISEASELQEELALLELKKKLLdAFLS 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  260 KersvleSSLKDLESKLSTSQEDgsklsDLNAecmdlrnrvEHLQVlLDKATKQADQAiRVLQQNQELQ---EKVEKLEE 336
Cdd:smart01087  92 K------FTLSQDELDVLTSREG-----PIDD---------EFFQV-LDKVQEIHEDC-SVLLQNEYQTaglEIMEKMNQ 149

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1731025460  337 SLEKANvfklssEKLQQ--ENELmqqkIDLLEDRLQSSDEELQSYIKLYQESVKeFQDTLDTI 397
Cdd:smart01087 150 LLERAY------ERLYRwlQSEL----RNLTTDNPEILSLLRQALRRLSERPVL-FKYCLDEF 201

Laminin_I

pfam06008

Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ...

231-402

6.22e-03

Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.

Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 39.70 E-value: 6.22e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 231 NIVLKNDIQTLKEELSNVKNADQHLAFLEKERSVLESSLKDLESKLSTSQEDGSKLsdlNAECMDLRNRvehlqvlldka 310
Cdd:pfam06008  18 NYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQV---NAESERTLGH----------- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 311 TKQADQAIRVLQQN-QELQEKVEKLEEslekaNVFKLSSEKLQQENELMQQKIDLLEDR-----LQSSDEELQSYIKLY- 383
Cdd:pfam06008  84 AKELAEAIKNLIDNiKEINEKVATLGE-----NDFALPSSDLSRMLAEAQRMLGEIRSRdfgtqLQNAEAELKAAQDLLs 158

                         170       180
                  ....*....|....*....|.
gi 1731025460 384 --QESVKEFQDTLDTIKKASK 402
Cdd:pfam06008 159 riQTWFQSPQEENKALANALR 179

Smc

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

258-408

6.25e-03

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.69 E-value: 6.25e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 258 LEKERSV------LESSLKDLESKLStsqedGSKLSDLNAECMDLRNRVEHLQVLLDKATKQADQA-IRVLQQNQELQEK 330
Cdd:COG1196   205 LERQAEKaeryreLKEELKELEAELL-----LLKLRELEAELEELEAELEELEAELEELEAELAELeAELEELRLELEEL 279

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1731025460 331 VEKLEESLEKANVFKLSSEKLQQENELMQQKIDLLEDRLQSSDEELQSYIKLYQESVKEFQDTLDTIKKASKKTATDE 408
Cdd:COG1196   280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE 357

OmpH

pfam03938

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

309-408

6.32e-03

Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 37.94 E-value: 6.32e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460 309 KATKQADQAIRvlQQNQELQEKVEKLEESLEKAnvfklsSEKLQQENELMQQKIDLLEDRLQSSDEELQSYIK-----LY 383
Cdd:pfam03938  15 PEGKAAQAQLE--KKFKKRQAELEAKQKELQKL------YEELQKDGALLEEEREEKEQELQKKEQELQQLQQkaqqeLQ 86

                          90       100
                  ....*....|....*....|....*
gi 1731025460 384 QESVKEFQDTLDTIKKASKKTATDE 408
Cdd:pfam03938  87 KKQQELLQPIQDKINKAIKEVAKEK 111

MukB

COG3096

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...

138-410

6.73e-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: 40.32 E-value: 6.73e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  138 ARVR-ALEDLEKIlsekEELQREINGLEMRLAEtdtrievaaQEKVhVELLEDQFEELQKQLNFSSGTVQSMNGNLNDip 216
Cdd:COG3096    337 NLVQtALRQQEKI----ERYQEDLEELTERLEE---------QEEV-VEEAAEQLAEAEARLEAAEEEVDSLKSQLAD-- 400

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  217 idsLTKELHLLKSENIVLKNDIQTLKE--------ELSnVKNADQHLAFLEKERSVLESSLKDLESKLSTSQedgsklsd 288
Cdd:COG3096    401 ---YQQALDVQQTRAIQYQQAVQALEKaralcglpDLT-PENAEDYLAAFRAKEQQATEEVLELEQKLSVAD-------- 468

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731025460  289 lnaecmDLRNRVEHLQVLLDK---------ATKQADQAIR-------VLQQNQELQEKVEKLEESLEK-ANVFKLSSEKL 351
Cdd:COG3096    469 ------AARRQFEKAYELVCKiageversqAWQTARELLRryrsqqaLAQRLQQLRAQLAELEQRLRQqQNAERLLEEFC 542

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1731025460  352 QQENELMQQKIDL--LEDRLQSSDEELQSYIKLYQESVKEFQDTLDTIKKASKKTATDEPV 410
Cdd:COG3096    543 QRIGQQLDAAEELeeLLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPA 603

YhaN