|
Name |
Accession |
Description |
Interval |
E-value |
| CUT |
pfam02376 |
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ... |
1147-1224 |
9.41e-31 |
|
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in cooperation with the homeodomain, often found downstream of the CUT domain. Multiple copies of the CUT domain can exist in one protein.
Pssm-ID: 460543 Cd Length: 78 Bit Score: 116.15 E-value: 9.41e-31
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622917383 1147 MSPELDTYGITKRVKEVLTDNNLGQRLFGETILGLTQGSVSDLLARPKPWHKLSLKGREpFVRMQLWLNDPNNVEKLM 1224
Cdd:pfam02376 1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDERMEI 77
|
|
| CUT |
pfam02376 |
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ... |
964-1032 |
6.40e-28 |
|
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in cooperation with the homeodomain, often found downstream of the CUT domain. Multiple copies of the CUT domain can exist in one protein.
Pssm-ID: 460543 Cd Length: 78 Bit Score: 108.06 E-value: 6.40e-28
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622917383 964 MYQEVDTIELTRQVKEKLAKNGICQRIFGEKVLGLSQGSVSDMLSRPKPWSKLTQKGREpFIRMQLWLN 1032
Cdd:pfam02376 1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLS 68
|
|
| CUT |
pfam02376 |
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ... |
572-648 |
1.66e-26 |
|
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in cooperation with the homeodomain, often found downstream of the CUT domain. Multiple copies of the CUT domain can exist in one protein.
Pssm-ID: 460543 Cd Length: 78 Bit Score: 104.21 E-value: 1.66e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622917383 572 EGEEMDTAEIARQVKEQLIKHNIGQRIFGHYVLGLSQGSVSEILARPKPWNKLTVRGKEpFHKMKQFLSDEQNILAL 648
Cdd:pfam02376 1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDERME 76
|
|
| Homeodomain |
pfam00046 |
Homeodomain; |
1270-1326 |
1.02e-15 |
|
Homeodomain;
Pssm-ID: 459649 [Multi-domain] Cd Length: 57 Bit Score: 72.53 E-value: 1.02e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622917383 1270 KKPRVVLAPEEKEALKRAYQQKPYPSPKTIEDLATQLNLKTSTVINWFHNYRSRIRR 1326
Cdd:pfam00046 1 RRKRTTFTPEQLEELEKEFQENPYPSAEEREELAAQLGLTERQVKVWFQNRRAKWKR 57
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
121-425 |
3.71e-14 |
|
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: 78.17 E-value: 3.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 121 DLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVT----IKALKEKIREYEQTLKNQAETIALEkeQKLQND 196
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEElsrqISALRKDLARLEAEVEQLEERIAQL--SKELTE 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 197 FAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDE----------ETTAKADEIEMIMTDLERANQ 266
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDElraeltllneEAANLRERLESLERRIAATER 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 267 RAEVAQREAETLREQLSSANHSLqlasqiqkapdveqaievltrSSLEVELAAKEREIAQLVEDVQRLQASLTKLR---E 343
Cdd:TIGR02168 839 RLEDLEEQIEELSEDIESLAAEI---------------------EELEELIEELESELEALLNERASLEEALALLRselE 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 344 NSASQISQLEQQLSAKNSTLKQLEEKLkGQADYEEVKKELNILKSMEFAPSEGAGTQDAAKPLEVLLMEKNRSLQSENAA 423
Cdd:TIGR02168 898 ELSEELRELESKRSELRRELEELREKL-AQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKR 976
|
..
gi 1622917383 424 LR 425
Cdd:TIGR02168 977 LE 978
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
47-377 |
9.48e-14 |
|
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: 76.63 E-value: 9.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 47 NRQDESEQSRKRLIEQSREfKKNTPEDLRKQVAPL-LKSFQGEIDALSKRSKEAEaaflnvykRLIDvpdpvpalDLGQQ 125
Cdd:TIGR02168 199 ERQLKSLERQAEKAERYKE-LKAELRELELALLVLrLEELREELEELQEELKEAE--------EELE--------ELTAE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 126 LQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQ----EVTIKALKEKIREYEQTLKNQAETIALEKEQK--LQNDFAE 199
Cdd:TIGR02168 262 LQELEEKLEELRLEVSELEEEIEELQKELYALANEisrlEQQKQILRERLANLERQLEELEAQLEELESKLdeLAEELAE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 200 KERKLQETQMSTTS---KLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKAD---EIEMIMTDLERANQRAEVAQR 273
Cdd:TIGR02168 342 LEEKLEELKEELESleaELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASlnnEIERLEARLERLEDRRERLQQ 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 274 EAETLREQLSSAN---HSLQLASQIQKAPDVEQAIEVLTR--SSLEVELAAKEREIAQLVEDVQRLQASLTKLR------ 342
Cdd:TIGR02168 422 EIEELLKKLEEAElkeLQAELEELEEELEELQEELERLEEalEELREELEEAEQALDAAERELAQLQARLDSLErlqenl 501
|
330 340 350
....*....|....*....|....*....|....*
gi 1622917383 343 ENSASQISQLEQQLSAKNSTLKQLEEKLKGQADYE 377
Cdd:TIGR02168 502 EGFSEGVKALLKNQSGLSGILGVLSELISVDEGYE 536
|
|
| homeodomain |
cd00086 |
Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic ... |
1270-1327 |
6.44e-13 |
|
Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic developmental processes; may bind to DNA as monomers or as homo- and/or heterodimers, in a sequence-specific manner.
Pssm-ID: 238039 [Multi-domain] Cd Length: 59 Bit Score: 64.57 E-value: 6.44e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622917383 1270 KKPRVVLAPEEKEALKRAYQQKPYPSPKTIEDLATQLNLKTSTVINWFHNYRSRIRRE 1327
Cdd:cd00086 1 RRKRTRFTPEQLEELEKEFEKNPYPSREEREELAKELGLTERQVKIWFQNRRAKLKRS 58
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
96-422 |
1.46e-12 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 72.30 E-value: 1.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 96 SKEAEAAFLNVYKRLIDVPDPVPALdlgQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVT-----IKALKEK 170
Cdd:COG5185 221 LLEKAKEIINIEEALKGFQDPESEL---EDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANnlikqFENTKEK 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 171 IREYEQTLKNQAETIALEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYD-EETTA 249
Cdd:COG5185 298 IAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVElSKSSE 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 250 KAD-----------EIEMIMTDLERANQRAE--------VAQREAETLREQLSSANHSLQLASQIQKA-----PDVEQAI 305
Cdd:COG5185 378 ELDsfkdtiestkeSLDEIPQNQRGYAQEILatledtlkAADRQIEELQRQIEQATSSNEEVSKLLNEliselNKVMREA 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 306 EVLTRSSLEVELAAKEREIAQ----LVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKLKGQADYEEvkk 381
Cdd:COG5185 458 DEESQSRLEEAYDEINRSVRSkkedLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARG--- 534
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1622917383 382 ELNILKSMEFAPSEGAGTQDAAKPLEVLLMEKNRSLQSENA 422
Cdd:COG5185 535 YAHILALENLIPASELIQASNAKTDGQAANLRTAVIDELTQ 575
|
|
| HOX |
smart00389 |
Homeodomain; DNA-binding factors that are involved in the transcriptional regulation of key ... |
1270-1325 |
3.70e-12 |
|
Homeodomain; DNA-binding factors that are involved in the transcriptional regulation of key developmental processes
Pssm-ID: 197696 [Multi-domain] Cd Length: 57 Bit Score: 62.65 E-value: 3.70e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622917383 1270 KKPRVVLAPEEKEALKRAYQQKPYPSPKTIEDLATQLNLKTSTVINWFHNYRSRIR 1325
Cdd:smart00389 2 RRKRTSFTPEQLEELEKEFQKNPYPSREEREELAKKLGLSERQVKVWFQNRRAKWK 57
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
125-383 |
6.88e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.74 E-value: 6.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 125 QLQLKVQRLHDIETENQKLRETLEEYNKEFAEvknQEVTIKALKEKIREYEQTLKNQAETIalekeQKLQNDFAEKERKL 204
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEE---LEAELAELEAELEELRLELEELELEL-----EEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 205 QEtqmsttskLEEAEHKVQSLQTALEKTRTELfdlktkyDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSS 284
Cdd:COG1196 298 AR--------LEQDIARLEERRRELEERLEEL-------EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 285 ANHSLQLASQIQKApdveqaiEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLK 364
Cdd:COG1196 363 AEEALLEAEAELAE-------AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE 435
|
250
....*....|....*....
gi 1622917383 365 QLEEKLKGQADYEEVKKEL 383
Cdd:COG1196 436 EEEEEEEALEEAAEEEAEL 454
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
47-388 |
1.00e-10 |
|
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: 66.58 E-value: 1.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 47 NRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQgEIDALSKRSKEAEAAFLNVYKRLIDVPDPVPAL-----D 121
Cdd:TIGR04523 165 KKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLS-NLKKKIQKNKSLESQISELKKQNNQLKDNIEKKqqeinE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 122 LGQQLQLKVQRLHDIETENQKLRETLEEYNKEfaeVKNQEVTIKALKEKIreyeQTLKNQAETIALEKEQKLQNDFAE-- 199
Cdd:TIGR04523 244 KTTEISNTQTQLNQLKDEQNKIKKQLSEKQKE---LEQNNKKIKELEKQL----NQLKSEISDLNNQKEQDWNKELKSel 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 200 --KERKLQETQmsttSKLEEAEHKVQSLQ---TALEKTRTELFDLKTKYDEETTAKADEIEmimtDLERANQRaevAQRE 274
Cdd:TIGR04523 317 knQEKKLEEIQ----NQISQNNKIISQLNeqiSQLKKELTNSESENSEKQRELEEKQNEIE----KLKKENQS---YKQE 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 275 AETLREQLSSanhslqLASQIQKAPDVEQaievltrsSLEVELAAKEREIAQLVEDVQRLQASLTKLrensASQISQLEQ 354
Cdd:TIGR04523 386 IKNLESQIND------LESKIQNQEKLNQ--------QKDEQIKKLQQEKELLEKEIERLKETIIKN----NSEIKDLTN 447
|
330 340 350
....*....|....*....|....*....|....*
gi 1622917383 355 QLSAKNSTLKQLEEKLKGQADY-EEVKKELNILKS 388
Cdd:TIGR04523 448 QDSVKELIIKNLDNTRESLETQlKVLSRSINKIKQ 482
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
34-389 |
1.08e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 66.63 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 34 IKRELDATATVLANRQDESEQsRKRLIEQSREFKKNTP-------EDLRKQvapLLKSFQGEIDALSKRSKEAEAAFLNV 106
Cdd:PRK03918 403 IEEEISKITARIGELKKEIKE-LKKAIEELKKAKGKCPvcgreltEEHRKE---LLEEYTAELKRIEKELKEIEEKERKL 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 107 YKRLIDVpdpvpalDLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEvtIKALKEKIREYEQTLKNQAETia 186
Cdd:PRK03918 479 RKELREL-------EKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEE--YEKLKEKLIKLKGEIKSLKKE-- 547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 187 LEKEQKLQNDFAEKERKLQETQmsttSKLEEAEHKVQSLQ-TALEKTRTELFDLKTKYDEETTAKADEIEmimtdLERAN 265
Cdd:PRK03918 548 LEKLEELKKKLAELEKKLDELE----EELAELLKELEELGfESVEELEERLKELEPFYNEYLELKDAEKE-----LEREE 618
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 266 QRAEVAQREAETLREQLSSANHSLQlasqiqkapDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQAsltklrens 345
Cdd:PRK03918 619 KELKKLEEELDKAFEELAETEKRLE---------ELRKELEELEKKYSEEEYEELREEYLELSRELAGLRA--------- 680
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1622917383 346 asQISQLEQQLSAKNSTLKQLEEKLKgqaDYEEVKKELNILKSM 389
Cdd:PRK03918 681 --ELEELEKRREEIKKTLEKLKEELE---EREKAKKELEKLEKA 719
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
119-348 |
1.61e-10 |
|
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: 64.79 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 119 ALDLGQQLQLKVQRLH-DIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIAL--EKEQKLQN 195
Cdd:COG4942 18 QADAAAEAEAELEQLQqEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEleKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 196 DFAEKERKLQET-----QMSTTSKLEEAEHKVQSLQTAlekTRTELFDLKTKYDEEttaKADEIEMIMTDLERANQRAEV 270
Cdd:COG4942 98 ELEAQKEELAELlralyRLGRQPPLALLLSPEDFLDAV---RRLQYLKYLAPARRE---QAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622917383 271 AQREAETLREQLSSANHSLQLASQIQKApdveqaievlTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQ 348
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQK----------LLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
86-425 |
5.66e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.02 E-value: 5.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 86 QGEIDALSKRSKEAEAAFLNVYKRLIDVPDPVPALDLGQQLQLKVQRLHDIETENQKLRETLEEYnkefaevKNQEVTIK 165
Cdd:COG4717 94 QEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEEL-------RELEEELE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 166 ALKEKIREYEQTLKNQAETIALEKEQKLQnDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKtkyDE 245
Cdd:COG4717 167 ELEAELAELQEELEELLEQLSLATEEELQ-DLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA---LE 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 246 ETTAKADEIEMIMT--------DLERANQRAEVAqrEAETLREQLSSANHSLQLASQIQKAPDVEQAIEVLTRSSLE--- 314
Cdd:COG4717 243 ERLKEARLLLLIAAallallglGGSLLSLILTIA--GVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEeee 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 315 ---------VELAAKEREIAQLVEDVQRLQASLTKLRE-NSASQISQLEQQLS-----AKNSTLKQLEEKLKGQADYEEV 379
Cdd:COG4717 321 leellaalgLPPDLSPEELLELLDRIEELQELLREAEElEEELQLEELEQEIAallaeAGVEDEEELRAALEQAEEYQEL 400
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1622917383 380 KKELNILKSmEFAPSEGAGTQDAAKPLEVLLMEKNRSLQSENAALR 425
Cdd:COG4717 401 KEELEELEE-QLEELLGELEELLEALDEEELEEELEELEEELEELE 445
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
34-386 |
1.08e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.16 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 34 IKRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQGEidALSKRSKEAEaaflNVYKRLIDV 113
Cdd:PRK03918 464 IEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLE--ELEKKAEEYE----KLKEKLIKL 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 114 PdpvpaldlGQQLQLK--VQRLHDIETENQKLRETLEEYNKEFAEVKNQEV-----TIKALKEKIREYEQtlknqaetiA 186
Cdd:PRK03918 538 K--------GEIKSLKkeLEKLEELKKKLAELEKKLDELEEELAELLKELEelgfeSVEELEERLKELEP---------F 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 187 LEKEQKLQNDFAEKERKLQEtQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEiemIMTDLERANQ 266
Cdd:PRK03918 601 YNEYLELKDAEKELEREEKE-LKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELRE---EYLELSRELA 676
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 267 RAEvaqREAETLREQLSSANHSLQlasqiqkapDVEQAIEVLTRSSLEVELAAKERE-IAQLVEDVQRLQAsltKLRENS 345
Cdd:PRK03918 677 GLR---AELEELEKRREEIKKTLE---------KLKEELEEREKAKKELEKLEKALErVEELREKVKKYKA---LLKERA 741
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1622917383 346 ASQISQLEQQLSAK-------NSTLKQLEEKLKGQADYEEVKKELNIL 386
Cdd:PRK03918 742 LSKVGEIASEIFEEltegkysGVRVKAEENKVKLFVVYQGKERPLTFL 789
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
124-297 |
1.24e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.86 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 124 QQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKNQAETIALEKEQKLQNDFAEKERK 203
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAE---LEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 204 LQETQMSttskLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAK----ADEIEMIMTDLERANQRAEVAQREAETLR 279
Cdd:COG4717 151 LEERLEE----LRELEEELEELEAELAELQEELEELLEQLSLATEEElqdlAEELEELQQRLAELEEELEEAQEELEELE 226
|
170
....*....|....*...
gi 1622917383 280 EQLSSANHSLQLASQIQK 297
Cdd:COG4717 227 EELEQLENELEAAALEER 244
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
50-371 |
5.17e-09 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 59.54 E-value: 5.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 50 DESEQSRKRLIEQSREFKKNtpedlRKQVAPLLKSFQGEIDALSKRSKEaeaaFLNVYKRLIDVPDpvpalDLGQQLQ-L 128
Cdd:COG1340 11 EELEEKIEELREEIEELKEK-----RDELNEELKELAEKRDELNAQVKE----LREEAQELREKRD-----ELNEKVKeL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 129 KVQRLhDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLknQAETIALEKEQKLQNDFAEKERKLQETQ 208
Cdd:COG1340 77 KEERD-ELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQ--QTEVLSPEEEKELVEKIKELEKELEKAK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 209 msttsKLEEAEHKVQSLQTALEKTRTELFDLKTKYdEETTAKADEIEMIMTDLeranqraevaQREAETLREQLSSANHS 288
Cdd:COG1340 154 -----KALEKNEKLKELRAELKELRKEAEEIHKKI-KELAEEAQELHEEMIEL----------YKEADELRKEADELHKE 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 289 LQLASQiqkapdveqaievltrsslevELAAKEREIAQLVEDVQRLQASLTKLRENSASqiSQLEQQLSAKNSTLKQLEE 368
Cdd:COG1340 218 IVEAQE---------------------KADELHEEIIELQKELRELRKELKKLRKKQRA--LKREKEKEELEEKAEEIFE 274
|
...
gi 1622917383 369 KLK 371
Cdd:COG1340 275 KLK 277
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
131-388 |
5.63e-09 |
|
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: 61.24 E-value: 5.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 131 QRLHDIETENQKLRETLEEYNKEfaevKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQNDFAEKERKLQ----- 205
Cdd:TIGR02169 184 ENIERLDLIIDEKRQQLERLRRE----REKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEkltee 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 206 ---------------------------ETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLK---TKYDEETTAKADEIE 255
Cdd:TIGR02169 260 iselekrleeieqlleelnkkikdlgeEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEerlAKLEAEIDKLLAEIE 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 256 MIMTDLERANQR-----AEVAQREAE--TLREQLSSANHSLQLASQIQKapDVEQAIEVLTR---------SSLEVELAA 319
Cdd:TIGR02169 340 ELEREIEEERKRrdkltEEYAELKEEleDLRAELEEVDKEFAETRDELK--DYREKLEKLKReinelkrelDRLQEELQR 417
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622917383 320 KEREIAQLVEDVQRLQASLTKL---RENSASQISQLEQQLSAKNSTLKQLEEKL-KGQADYEEVKKELNILKS 388
Cdd:TIGR02169 418 LSEELADLNAAIAGIEAKINELeeeKEDKALEIKKQEWKLEQLAADLSKYEQELyDLKEEYDRVEKELSKLQR 490
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
142-452 |
7.43e-09 |
|
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: 60.85 E-value: 7.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 142 KLRETLEEYNKEFAEVKNQEVTIKALKEKIR----EYEQTLKN-QAETIALEKEQKLqndFAEKERKLQEtqmsttsKLE 216
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIEnrldELSQELSDaSRKIGEIEKEIEQ---LEQEEEKLKE-------RLE 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 217 EAEHKVQSLQTALEKTRTELFDLKTKYdEETTAKADEIEMIMTDLER--ANQRAEVAQREAETLREQLSSANHSLQlasq 294
Cdd:TIGR02169 741 ELEEDLSSLEQEIENVKSELKELEARI-EELEEDLHKLEEALNDLEArlSHSRIPEIQAELSKLEEEVSRIEARLR---- 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 295 iqkapdveqaievltrsSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSAS----------QISQLEQQLSAKNSTLK 364
Cdd:TIGR02169 816 -----------------EIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSiekeienlngKKEELEEELEELEAALR 878
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 365 QLEEKLKG-QADYEEVKKELNILksmefapsegagtQDAAKPLEVLLMEKNRSLQSENAALRISNSDLSGSARRKGKDQP 443
Cdd:TIGR02169 879 DLESRLGDlKKERDELEAQLREL-------------ERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEE 945
|
....*....
gi 1622917383 444 ESRRPGSLP 452
Cdd:TIGR02169 946 IPEEELSLE 954
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
155-396 |
8.18e-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: 59.39 E-value: 8.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 155 AEVKNQEVTIKALKEKIREYEQTLKNQAETI--ALEKEQKLQNDFAEKERKLQETQmsttSKLEEAEHKVQSLQTALEKT 232
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEkaLLKQLAALERRIAALARRIRALE----QELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 233 RTELFDLKTKYDE-----ETTAKADEIEMIM--TDLERANQRAEVAQREAETLREQLSsanhslQLASQIQKAPDVEQAI 305
Cdd:COG4942 96 RAELEAQKEELAEllralYRLGRQPPLALLLspEDFLDAVRRLQYLKYLAPARREQAE------ELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 306 EVlTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRensaSQISQLEQQLSAKNSTLKQLEEKLKGQAdyEEVKKELNI 385
Cdd:COG4942 170 EA-ERAELEALLAELEEERAALEALKAERQKLLARLE----KELAELAAELAELQQEAEELEALIARLE--AEAAAAAER 242
|
250
....*....|.
gi 1622917383 386 LKSMEFAPSEG 396
Cdd:COG4942 243 TPAAGFAALKG 253
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
34-374 |
8.93e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.34 E-value: 8.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 34 IKRELDATATVLANRQDESEQSRKRLIEQSREFkkntpEDLRKQVAPLLKS---FQGEIDALSKRSKEAEAAFLNVYKRL 110
Cdd:COG1196 251 LEAELEELEAELAELEAELEELRLELEELELEL-----EEAQAEEYELLAElarLEQDIARLEERRRELEERLEELEEEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 111 idvpdpvpaLDLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEvtiKALKEKIREYEQTLKNQAEtiALEKE 190
Cdd:COG1196 326 ---------AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL---LEAEAELAEAEEELEELAE--ELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 191 QKLQNDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEmimtdlERANQRAEV 270
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE------EEEALLELL 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 271 AQ--REAETLREQLSSANHSL-QLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSAS 347
Cdd:COG1196 466 AEllEEAALLEAALAELLEELaEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALA 545
|
330 340
....*....|....*....|....*..
gi 1622917383 348 qiSQLEQQLSAKNSTLKQLEEKLKGQA 374
Cdd:COG1196 546 --AALQNIVVEDDEVAAAAIEYLKAAK 570
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
74-441 |
1.18e-08 |
|
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: 59.98 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 74 LRKQVAPLLKSFQGEIDALSKRSK---EAEAAFLNVYKRLIDVPDPVPALDLGQQLQLKVQRLHDIETENQKLRETLEEY 150
Cdd:TIGR00618 554 ERKQRASLKEQMQEIQQSFSILTQcdnRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLH 633
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 151 NKEFAEVKNQEVTIKAlkekirEYEQTLKNQAETIALE--KEQKLQNdFAEKERKLQETQ---MSTTSKLEEAEHKvqsl 225
Cdd:TIGR00618 634 LQQCSQELALKLTALH------ALQLTLTQERVREHALsiRVLPKEL-LASRQLALQKMQsekEQLTYWKEMLAQC---- 702
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 226 QTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAET-LREQ-LSSANHSLQLASQIQKAPDVEQ 303
Cdd:TIGR00618 703 QTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTvLKARtEAHFNNNEEVTAALQTGAELSH 782
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 304 AIEVLT-----RSSLEVELAAKEREIAQLVED------------VQRLQASLTKLRENSASQIsQLEQQLSAKNSTLKQL 366
Cdd:TIGR00618 783 LAAEIQffnrlREEDTHLLKTLEAEIGQEIPSdedilnlqcetlVQEEEQFLSRLEEKSATLG-EITHQLLKYEECSKQL 861
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622917383 367 EEKLKGQADYEEVKKELNILKSMEFAPSEGAGTQDAAKplevLLMEKNRSLQSENAALRISNSDLSGSARRKGKD 441
Cdd:TIGR00618 862 AQLTQEQAKIIQLSDKLNGINQIKIQFDGDALIKFLHE----ITLYANVRLANQSEGRFHGRYADSHVNARKYQG 932
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
186-382 |
1.57e-08 |
|
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: 58.62 E-value: 1.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 186 ALEKEQKLQNDFAEKERKLQETQmsttSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEettaKADEIEMIMTDLERAN 265
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELE----KELAALKKEEKALLKQLAALERRIAALARRIRA----LEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 266 QRAEVAQREAETLREQLSSANHSLQLASQIQK------APDVEQAIEVLT--------RSSLEVELAAKEREIAQLVEDV 331
Cdd:COG4942 90 KEIAELRAELEAQKEELAELLRALYRLGRQPPlalllsPEDFLDAVRRLQylkylapaRREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1622917383 332 QRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKLKGQADYEEVKKE 382
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
137-389 |
2.41e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.91 E-value: 2.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 137 ETENqKLRETLEEYNKefaevknqevtIKALKEKIREYEQTLKNQAEtiALEKEQKLQNDFAEKERKLQetqmstTSKLE 216
Cdd:TIGR02168 176 ETER-KLERTRENLDR-----------LEDILNELERQLKSLERQAE--KAERYKELKAELRELELALL------VLRLE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 217 EAEHKVQSLQTALEKTRTELFDLKTKYDEETTakadEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASqiQ 296
Cdd:TIGR02168 236 ELREELEELQEELKEAEEELEELTAELQELEE----KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILR--E 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 297 KAPDVEQAIEVLTRSSLEV---------ELAAKEREIAQLVEDVQRLQASLTKLR---ENSASQISQLEQQLSAKNSTLK 364
Cdd:TIGR02168 310 RLANLERQLEELEAQLEELeskldelaeELAELEEKLEELKEELESLEAELEELEaelEELESRLEELEEQLETLRSKVA 389
|
250 260
....*....|....*....|....*.
gi 1622917383 365 QLEEKLKG-QADYEEVKKELNILKSM 389
Cdd:TIGR02168 390 QLELQIASlNNEIERLEARLERLEDR 415
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
165-438 |
2.60e-08 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 58.83 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 165 KALKEKIREYEQTLKNQAETIALEK-EQKLQNDFAEKERKLQETQmsttsKLEEAEhkvqsLQTALEKTRTELFDLKTKY 243
Cdd:pfam02463 173 EALKKLIEETENLAELIIDLEELKLqELKLKEQAKKALEYYQLKE-----KLELEE-----EYLLYLDYLKLNEERIDLL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 244 DEETTAKADEIEMImtdleraNQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVEQAIEVLTRSSLEVELAAKERE 323
Cdd:pfam02463 243 QELLRDEQEEIESS-------KQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEK 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 324 IAQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKLKGQADYEEVKKELNILKSmefapSEGAGTQDAA 403
Cdd:pfam02463 316 LKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKK-----LESERLSSAA 390
|
250 260 270
....*....|....*....|....*....|....*
gi 1622917383 404 KPLEVLLMEKNRSLQSENAALRISNSDLSGSARRK 438
Cdd:pfam02463 391 KLKEEELELKSEEEKEAQLLLELARQLEDLLKEEK 425
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
33-435 |
3.00e-08 |
|
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: 58.70 E-value: 3.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 33 GIKRELDAtatVLANRQDESEQSRKRLIEQSREfKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLNVYKRLID 112
Cdd:pfam12128 582 GVKLDLKR---IDVPEWAASEEELRERLDKAEE-ALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRR 657
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 113 VpdpvpaLDLGQQLQLKVQRlhDIETENQKLRETLEEYNKEfaevknqevtIKALKEKIREYEQTLKNQAETIALEKEQK 192
Cdd:pfam12128 658 L------FDEKQSEKDKKNK--ALAERKDSANERLNSLEAQ----------LKQLDKKHQAWLEEQKEQKREARTEKQAY 719
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 193 LQNdfAEKERKLQETQMSTTSKLEEAEHKVQslQTALEKTRTElfDLKTK-YDEETTAK-ADEIEMIMTDLERANQRAEV 270
Cdd:pfam12128 720 WQV--VEGALDAQLALLKAAIAARRSGAKAE--LKALETWYKR--DLASLgVDPDVIAKlKREIRTLERKIERIAVRRQE 793
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 271 AQREAETLREQLSSANHSLQlasqIQKApDVEQAIEvltrsslevelaakereiaqlvedvqRLQASLTKLRENSASQIS 350
Cdd:pfam12128 794 VLRYFDWYQETWLQRRPRLA----TQLS-NIERAIS--------------------------ELQQQLARLIADTKLRRA 842
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 351 QLEQQLSAKNSTLKQLEEKLKGQADYEEVKKELNILKSMEFAPSEGAGTQDAAKPLEVLLMEKNRSLQSENAALRISNSD 430
Cdd:pfam12128 843 KLEMERKASEKQQVRLSENLRGLRCEMSKLATLKEDANSEQAQGSIGERLAQLEDLKLKRDYLSESVKKYVEHFKNVIAD 922
|
....*
gi 1622917383 431 LSGSA 435
Cdd:pfam12128 923 HSGSG 927
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
145-366 |
3.39e-08 |
|
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: 55.30 E-value: 3.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 145 ETLEEYNKEFAEVKN--QEVT------IKALKEKIREyeqtLKNQAEtialEKEQKLQNDFAEKERkLQEtqmsttsKLE 216
Cdd:pfam13851 1 ELMKNHEKAFNEIKNyyNDITrnnlelIKSLKEEIAE----LKKKEE----RNEKLMSEIQQENKR-LTE-------PLQ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 217 EAEHKVQSLQTAL---EKTRTELfdlktkydEETTAKADEIEMIMTDLERAN----QRAEVAQREAETLREQLSSANHSL 289
Cdd:pfam13851 65 KAQEEVEELRKQLenyEKDKQSL--------KNLKARLKVLEKELKDLKWEHevleQRFEKVERERDELYDKFEAAIQDV 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622917383 290 QLASQiQKAPDVEQAIEVLTRsslevELAAKEREIAQLvedvqrLQASltKLRENSASQISQ-LEQQLSAKNSTLKQL 366
Cdd:pfam13851 137 QQKTG-LKNLLLEKKLQALGE-----TLEKKEAQLNEV------LAAA--NLDPDALQAVTEkLEDVLESKNQLIKDL 200
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
35-313 |
5.21e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.14 E-value: 5.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 35 KRELDATATVLANRQDESEQSRKRLIEQSREF--KKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAflnvykrlid 112
Cdd:TIGR02168 297 ISRLEQQKQILRERLANLERQLEELEAQLEELesKLDELAEELAELEEKLEELKEELESLEAELEELEAE---------- 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 113 vpdpvpaldlgqqlqlkvqrLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKNQAETIALEKEQK 192
Cdd:TIGR02168 367 --------------------LEELESRLEELEEQLETLRSKVAQLELQ---IASLNNEIERLEARLERLEDRRERLQQEI 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 193 LQNDFAEKERKLQETQMSTTSK---LEEAEHKVQSLQTALEKTRTELFDLKTKYDeETTAKADEIEMIMTDLERANQRAE 269
Cdd:TIGR02168 424 EELLKKLEEAELKELQAELEELeeeLEELQEELERLEEALEELREELEEAEQALD-AAERELAQLQARLDSLERLQENLE 502
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1622917383 270 VAQRE-AETLREQLSSANHSLQLASQIQKAPDVEQAIEVLTRSSL 313
Cdd:TIGR02168 503 GFSEGvKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRL 547
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
51-387 |
5.41e-08 |
|
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: 57.72 E-value: 5.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 51 ESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLK---SFQGEIDALsKRSKEAEAAFLNVYKRLIDVPDPvPALDLGQQLQ 127
Cdd:TIGR04523 415 KKLQQEKELLEKEIERLKETIIKNNSEIKDLTNqdsVKELIIKNL-DNTRESLETQLKVLSRSINKIKQ-NLEQKQKELK 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 128 LKVQRLHDIETENQKLRETLEEYNKEFAEVKNqevTIKALKEKIREYEQTLKNQAETIaLEKEQKLQNDFAEKErkLQET 207
Cdd:TIGR04523 493 SKEKELKKLNEEKKELEEKVKDLTKKISSLKE---KIEKLESEKKEKESKISDLEDEL-NKDDFELKKENLEKE--IDEK 566
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 208 QmsttSKLEEAEHKvqslQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQ----LS 283
Cdd:TIGR04523 567 N----KEIEELKQT----QKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIikniKS 638
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 284 SANHSLQLASQIQ--------KAPDVEQAIEvltrsslevELAAKEREIAQLVEDvqRLQASLTKLRENSASQIsqleqq 355
Cdd:TIGR04523 639 KKNKLKQEVKQIKetikeirnKWPEIIKKIK---------ESKTKIDDIIELMKD--WLKELSLHYKKYITRMI------ 701
|
330 340 350
....*....|....*....|....*....|..
gi 1622917383 356 lsaKNSTLKQLEEKlkgqadYEEVKKELNILK 387
Cdd:TIGR04523 702 ---RIKDLPKLEEK------YKEIEKELKKLD 724
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
164-386 |
5.50e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.47 E-value: 5.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 164 IKALKEKIREYE-----QTLKNQAETIALEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRtelfd 238
Cdd:COG4717 48 LERLEKEADELFkpqgrKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE----- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 239 lktkydeettaKADEIEMIMTDLERANQRAEVAQREAETLREQLssanhsLQLASQIQKAPDVEQAIEVLTRS---SLEV 315
Cdd:COG4717 123 -----------KLLQLLPLYQELEALEAELAELPERLEELEERL------EELRELEEELEELEAELAELQEEleeLLEQ 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622917383 316 ELAAKEREIAQLVEDVQRLQASLTKLREnsasQISQLEQQLSAKNSTLKQLEEKLKGQADYEEVKKELNIL 386
Cdd:COG4717 186 LSLATEEELQDLAEELEELQQRLAELEE----ELEEAQEELEELEEELEQLENELEAAALEERLKEARLLL 252
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
131-278 |
5.81e-08 |
|
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: 55.32 E-value: 5.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 131 QRLHDIETENQKLRETLEEYNKEF----AEVKNQEVTIKALKEKIREYEQTL---KNQAETIALEKEQklqnDFAEKERK 203
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELedleKEIKRLELEIEEVEARIKKYEEQLgnvRNNKEYEALQKEI----ESLKRRIS 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622917383 204 LQETqmsttsKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERAN-QRAEVAQREAETL 278
Cdd:COG1579 107 DLED------EILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEaEREELAAKIPPEL 176
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
39-374 |
5.86e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 57.74 E-value: 5.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 39 DATATVLANRQDE----SEQSRKRLIEQ--SREFKKNTPEDLRKQVAPLlksfQGEIDALSKRSKEAEAAFLNVYKRLID 112
Cdd:PRK02224 306 DADAEAVEARREEledrDEELRDRLEECrvAAQAHNEEAESLREDADDL----EERAEELREEAAELESELEEAREAVED 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 113 VPDPVPALDlgQQLQLKVQRLHDIETEnqklRETLEEYNKEFAEVKNqevtikALKEKIREYEQTLKNQAETIAlEKEQK 192
Cdd:PRK02224 382 RREEIEELE--EEIEELRERFGDAPVD----LGNAEDFLEELREERD------ELREREAELEATLRTARERVE-EAEAL 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 193 LQ-NDFAEKERKLQETQMSTTskLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAK--ADEIEMIMTDLERANQRAE 269
Cdd:PRK02224 449 LEaGKCPECGQPVEGSPHVET--IEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVeaEDRIERLEERREDLEELIA 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 270 VAQREAETLREQLSSANHSLQ-LASQIQKAPDVEQAIEVLTRSSLEvELAAKEREIAQLVEDVQRLQ--ASLTKLRENSA 346
Cdd:PRK02224 527 ERRETIEEKRERAEELRERAAeLEAEAEEKREAAAEAEEEAEEARE-EVAELNSKLAELKERIESLEriRTLLAAIADAE 605
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1622917383 347 SQISQLEQQ--------------LSAKNSTLKQLEEKLKGQA 374
Cdd:PRK02224 606 DEIERLREKrealaelnderrerLAEKRERKRELEAEFDEAR 647
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
26-370 |
8.26e-08 |
|
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: 57.16 E-value: 8.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 26 AHWLcspgikRELDATATVLANR------QDESEQ----------------SRKRLIEQSREFKKNTPEDLRKQVAPLLK 83
Cdd:pfam12128 224 EHWI------RDIQAIAGIMKIRpeftklQQEFNTlesaelrlshlhfgykSDETLIASRQEERQETSAELNQLLRTLDD 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 84 SFQGEIDALSKRSKEAEAAFLNV----------YKRLIDVPDPVPALDLGQQLQLK-----VQRLHDIETENQklRETLE 148
Cdd:pfam12128 298 QWKEKRDELNGELSAADAAVAKDrselealedqHGAFLDADIETAAADQEQLPSWQselenLEERLKALTGKH--QDVTA 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 149 EYNKEFAEVKNQEVT----IKALKEKIREYEQTLKNQAETIALEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKVQS 224
Cdd:pfam12128 376 KYNRRRSKIKEQNNRdiagIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQ 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 225 LQ-TALEKTRTELFD-LKTKYDEETTAKADEIEMIMTD--------------LERANQRAEVAQREAETLREQLSSANHS 288
Cdd:pfam12128 456 ATaTPELLLQLENFDeRIERAREEQEAANAEVERLQSElrqarkrrdqaseaLRQASRRLEERQSALDELELQLFPQAGT 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 289 LqLASQIQKAPDVEQAI------EVLTRSSLEVEL----AAKEREIAQLVEDVQRLQA-SLTKLRENSASQISQLEQQLS 357
Cdd:pfam12128 536 L-LHFLRKEAPDWEQSIgkvispELLHRTDLDPEVwdgsVGGELNLYGVKLDLKRIDVpEWAASEEELRERLDKAEEALQ 614
|
410
....*....|...
gi 1622917383 358 AKNSTLKQLEEKL 370
Cdd:pfam12128 615 SAREKQAAAEEQL 627
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
133-387 |
1.33e-07 |
|
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: 56.37 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 133 LHDIETENQKLRETLEEYNK---EFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQNDFAEKERKLQETQM 209
Cdd:pfam10174 201 LDQKEKENIHLREELHRRNQlqpDPAKTKALQTVIEMKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEVY 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 210 STTSKLeeAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKAD---EIEMIMTDLERANQRAEVAQREAETLREQLSSAN 286
Cdd:pfam10174 281 KSHSKF--MKNKIDQLKQELSKKESELLALQTKLETLTNQNSDckqHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 287 HSLQ---------------LASQIQKAPDV----EQAIEVLTR--SSLEVELAAKEREIAQLVEDVQRLQASLTklreNS 345
Cdd:pfam10174 359 SFLNkktkqlqdlteekstLAGEIRDLKDMldvkERKINVLQKkiENLQEQLRDKDKQLAGLKERVKSLQTDSS----NT 434
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1622917383 346 ASQISQLEQQLSAKNSTLKQLEEK--LKGQADYEEV---KKELNILK 387
Cdd:pfam10174 435 DTALTTLEEALSEKERIIERLKEQreREDRERLEELeslKKENKDLK 481
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
186-384 |
1.75e-07 |
|
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: 53.78 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 186 ALEKEQKLQNDFAEKERKLQETQMsttsKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEettaKADEIEMIMTDLERAN 265
Cdd:COG1579 8 ALLDLQELDSELDRLEHRLKELPA----ELAELEDELAALEARLEAAKTELEDLEKEIKR----LELEIEEVEARIKKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 266 QRAEVA--QREAETLREQLSSanhslqLASQIQKAPDVEQAievltrssLEVELAAKEREIAQLVEDVQRLQASLTKLRE 343
Cdd:COG1579 80 EQLGNVrnNKEYEALQKEIES------LKRRISDLEDEILE--------LMERIEELEEELAELEAELAELEAELEEKKA 145
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1622917383 344 NSASQISQLEQQLSAKNSTLKQLEEKLKGQ--ADYEEVKKELN 384
Cdd:COG1579 146 ELDEELAELEAELEELEAEREELAAKIPPEllALYERIRKRKN 188
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
110-389 |
1.96e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.79 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 110 LIDVPDPVPALDLGQQLQLKVQrlhDIETENQKLR---------ETLEEYNKEFAEVKNQEVTIKALKEKIreyeqTLKN 180
Cdd:COG3206 60 LVEPQSSDVLLSGLSSLSASDS---PLETQIEILKsrpvlervvDKLNLDEDPLGEEASREAAIERLRKNL-----TVEP 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 181 QAETIAL---------EKEQKLQNDFAE------KERKLQETQMSTT---SKLEEAEHKVQSLQTALE--KTRTELFDLk 240
Cdd:COG3206 132 VKGSNVIeisytspdpELAAAVANALAEayleqnLELRREEARKALEfleEQLPELRKELEEAEAALEefRQKNGLVDL- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 241 tkyDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSanhSLQLASQIQKAPDVEQAIEVLtrSSLEVELA-- 318
Cdd:COG3206 211 ---SEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGS---GPDALPELLQSPVIQQLRAQL--AELEAELAel 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 319 ------------AKEREIA----QLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKlkgQADYEEVKKE 382
Cdd:COG3206 283 sarytpnhpdviALRAQIAalraQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPEL---EAELRRLERE 359
|
....*..
gi 1622917383 383 LNILKSM 389
Cdd:COG3206 360 VEVAREL 366
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
120-341 |
1.98e-07 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 55.79 E-value: 1.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 120 LDLGQQlQLKVQRLHdIETENQKLRETLEEYNKEFAEVKNQEVTIKA----LKEKIREYEQTLKNQAETIalekeQKLQN 195
Cdd:PHA02562 190 IDHIQQ-QIKTYNKN-IEEQRKKNGENIARKQNKYDELVEEAKTIKAeieeLTDELLNLVMDIEDPSAAL-----NKLNT 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 196 DFAEKERKLQ----ETQMST--------TSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETtakadeiemimtdlER 263
Cdd:PHA02562 263 AAAKIKSKIEqfqkVIKMYEkggvcptcTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELE--------------EI 328
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622917383 264 ANQRAEvAQREAETLREQLSSANHSLQLAsqIQKAPDVEQAIEvltrsSLEVELAAKEREIAQLVEDVQRLQASLTKL 341
Cdd:PHA02562 329 MDEFNE-QSKKLLELKNKISTNKQSLITL--VDKAKKVKAAIE-----ELQAEFVDNAEELAKLQDELDKIVKTKSEL 398
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
124-284 |
2.05e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.08 E-value: 2.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 124 QQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQNDFAEKERK 203
Cdd:COG4913 274 LEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERE 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 204 LQETQmsttSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLS 283
Cdd:COG4913 354 LEERE----RRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
|
.
gi 1622917383 284 S 284
Cdd:COG4913 430 S 430
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
50-390 |
2.48e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.46 E-value: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 50 DESEQSRKRLIEQSREFKKNTPEDLRKqvapllksfqgEIDALSKRSKEAEAAFLNVYKRLIDVPDpvpaldLGQQLQLK 129
Cdd:PRK03918 365 EEAKAKKEELERLKKRLTGLTPEKLEK-----------ELEELEKAKEEIEEEISKITARIGELKK------EIKELKKA 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 130 VQRLHDIE----------TENQKLrETLEEYNKEFAEVKNQEVTIKALKEKIR----EYEQTLKNQAETIALEK------ 189
Cdd:PRK03918 428 IEELKKAKgkcpvcgrelTEEHRK-ELLEEYTAELKRIEKELKEIEEKERKLRkelrELEKVLKKESELIKLKElaeqlk 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 190 --EQKLQNDFAEK-ERKLQE----------------TQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAK 250
Cdd:PRK03918 507 elEEKLKKYNLEElEKKAEEyeklkekliklkgeikSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFES 586
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 251 ADEIEMIMTDLER----------ANQRAEVAQREAETLREQLSSANHSLQLASqiQKAPDVEQAIEVLTRSSLEVELAAK 320
Cdd:PRK03918 587 VEELEERLKELEPfyneylelkdAEKELEREEKELKKLEEELDKAFEELAETE--KRLEELRKELEELEKKYSEEEYEEL 664
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622917383 321 EREIAQLVEDVQRLQA---SLTKLRENSASQISQLEQQLSAKNSTLKQLEEKLKGQADYEEVKKELNILKSME 390
Cdd:PRK03918 665 REEYLELSRELAGLRAeleELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALL 737
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
246-428 |
2.78e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.69 E-value: 2.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 246 ETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVEQAIEVLTRS----SLEVELAAKE 321
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQrrleLLEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 322 REIAQLVEDVQRLQASLTKLRE-----------NSASQISQLEQQLSAKNSTLKQLEEKLK---------------GQAD 375
Cdd:COG4913 302 AELARLEAELERLEARLDALREeldeleaqirgNGGDRLEQLEREIERLERELEERERRRArleallaalglplpaSAEE 381
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622917383 376 YEEVKKELNILKsmEFAPSEGAGTQDAAKPLEVLLMEKNR---SLQSENAAL--RISN 428
Cdd:COG4913 382 FAALRAEAAALL--EALEEELEALEEALAEAEAALRDLRRelrELEAEIASLerRKSN 437
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
165-369 |
3.39e-07 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 55.02 E-value: 3.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 165 KALKEKIREYEQTLKNQAETIALEKEQ-KLQNDFAEKERKL-----QETQMSTTSKLEEAE-HKVQ--SLQT-------- 227
Cdd:PHA02562 170 KLNKDKIRELNQQIQTLDMKIDHIQQQiKTYNKNIEEQRKKngeniARKQNKYDELVEEAKtIKAEieELTDellnlvmd 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 228 ------ALEKTRTELFDLKTKYdeETTAKadEIEMI---------MTDLERANQRaevaqreAETLREQLSSANHSL-QL 291
Cdd:PHA02562 250 iedpsaALNKLNTAAAKIKSKI--EQFQK--VIKMYekggvcptcTQQISEGPDR-------ITKIKDKLKELQHSLeKL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 292 ASQIQKAPDVEQAIEVLTRSSLEV--ELAAKEREIAQLVEDVQRLQASLTKL---RENSASQISQLEQQLSAKNSTLKQL 366
Cdd:PHA02562 319 DTAIDELEEIMDEFNEQSKKLLELknKISTNKQSLITLVDKAKKVKAAIEELqaeFVDNAEELAKLQDELDKIVKTKSEL 398
|
...
gi 1622917383 367 EEK 369
Cdd:PHA02562 399 VKE 401
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
72-264 |
3.55e-07 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 53.91 E-value: 3.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 72 EDLRKQVAPLLKSFQGEIDALSKRSKEAEAAfLNVYKRLIDVpdpvpaldlgQQLQLK--VQRLHDI-ETENQKL-RETL 147
Cdd:cd22656 113 EEAKKTIKALLDDLLKEAKKYQDKAAKVVDK-LTDFENQTEK----------DQTALEtlEKALKDLlTDEGGAIaRKEI 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 148 EEYNKEFAevKNQEVTIKALKEKIREYEQTLKNQAETIAleKEQKLQNDFaekerKLQETQM-STTSKLEEAEHKVQSLQ 226
Cdd:cd22656 182 KDLQKELE--KLNEEYAAKLKAKIDELKALIADDEAKLA--AALRLIADL-----TAADTDLdNLLALIGPAIPALEKLQ 252
|
170 180 190
....*....|....*....|....*....|....*...
gi 1622917383 227 TALEKTRTELFDLKTKYDEETTaKADEIEMIMTDLERA 264
Cdd:cd22656 253 GAWQAIATDLDSLKDLLEDDIS-KIPAAILAKLELEKA 289
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
176-384 |
5.14e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.68 E-value: 5.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 176 QTLKNQAETIALEKEQK-LQNDFAEKERKLQETQmSTTSKLEEAEHKVQSL----------------------------Q 226
Cdd:TIGR02168 671 SILERRREIEELEEKIEeLEEKIAELEKALAELR-KELEELEEELEQLRKEleelsrqisalrkdlarleaeveqleerI 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 227 TALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASqiQKAPDVEQAIE 306
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLN--EEAANLRERLE 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 307 VLTR--SSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKlkgQADYEEVKKELN 384
Cdd:TIGR02168 828 SLERriAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALL---RSELEELSEELR 904
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
51-388 |
6.46e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.30 E-value: 6.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 51 ESEQSRKRLIEQSREFKKNtpEDLRKQVAPLLKSFQGEIDALSKRSKEAEaaflNVYKRLIDVpdpvpaldlGQQLQLKV 130
Cdd:PRK03918 142 ESDESREKVVRQILGLDDY--ENAYKNLGEVIKEIKRRIERLEKFIKRTE----NIEELIKEK---------EKELEEVL 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 131 QRLHDIETENQKLRETLEEYNKEFAEV----------------------------KNQEVTIKALKEKIREYEQTLKNQA 182
Cdd:PRK03918 207 REINEISSELPELREELEKLEKEVKELeelkeeieelekeleslegskrkleekiRELEERIEELKKEIEELEEKVKELK 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 183 ETIALEKE----QKLQNDFAEKERKLQETQMSTT----------SKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETT 248
Cdd:PRK03918 287 ELKEKAEEyiklSEFYEEYLDELREIEKRLSRLEeeingieeriKELEEKEERLEELKKKLKELEKRLEELEERHELYEE 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 249 AKA--------------DEIEMIMTDLERANQRAEVAQREAETLREQLSSANH---SLQLA-SQIQKAP----------D 300
Cdd:PRK03918 367 AKAkkeelerlkkrltgLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKeikELKKAiEELKKAKgkcpvcgrelT 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 301 VEQAIEVLTRSSLEV--------ELAAKEREI---AQLVEDVQRLQASLTKLREnSASQISQLEQQLSAKNstLKQLEEK 369
Cdd:PRK03918 447 EEHRKELLEEYTAELkriekelkEIEEKERKLrkeLRELEKVLKKESELIKLKE-LAEQLKELEEKLKKYN--LEELEKK 523
|
410
....*....|....*....
gi 1622917383 370 LKgqaDYEEVKKELNILKS 388
Cdd:PRK03918 524 AE---EYEKLKEKLIKLKG 539
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
123-371 |
7.08e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.28 E-value: 7.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 123 GQQLQLKVQrlhdIE-TENQKLRETLEEYNKEFAEVKNQevtIKALKEKiREYEQTLKNQAETIALEKEQKLQ--NDFAE 199
Cdd:PRK02224 187 GSLDQLKAQ----IEeKEEKDLHERLNGLESELAELDEE---IERYEEQ-REQARETRDEADEVLEEHEERREelETLEA 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 200 KERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLK-----TKYDEETTAK-----ADEIEMIMTDLERANQRAE 269
Cdd:PRK02224 259 EIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLaeaglDDADAEAVEArreelEDRDEELRDRLEECRVAAQ 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 270 VAQREAETLRE---QLSSANHSLQlasqiQKAPDVEQAIEvltrsSLEVELAAKEREIAQLVEDVQRLQASLTKL---RE 343
Cdd:PRK02224 339 AHNEEAESLREdadDLEERAEELR-----EEAAELESELE-----EAREAVEDRREEIEELEEEIEELRERFGDApvdLG 408
|
250 260
....*....|....*....|....*...
gi 1622917383 344 NSASQISQLEQQLSAKNSTLKQLEEKLK 371
Cdd:PRK02224 409 NAEDFLEELREERDELREREAELEATLR 436
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
139-387 |
7.98e-07 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 54.21 E-value: 7.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 139 ENQKLRETLE---EYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQNDFAEKERKLQETQMSTTSKL 215
Cdd:pfam02463 174 ALKKLIEETEnlaELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEI 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 216 EEAEhKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREA--ETLREQLSSANHSLQLAS 293
Cdd:pfam02463 254 ESSK-QEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDeeKLKESEKEKKKAEKELKK 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 294 QIQKAPDVEQAIEVLTRSSLEVELA--AKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKN------STLKQ 365
Cdd:pfam02463 333 EKEEIEELEKELKELEIKREAEEEEeeELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSeeekeaQLLLE 412
|
250 260
....*....|....*....|..
gi 1622917383 366 LEEKLKGQADyEEVKKELNILK 387
Cdd:pfam02463 413 LARQLEDLLK-EEKKEELEILE 433
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
185-426 |
8.59e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.98 E-value: 8.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 185 IALEKEQKLQNDFAEKERKLQETQmsTTSKLEEAEHKVQSLQTALEKTRTELFDLKtkydEETTAKADEIEMIMTDLERA 264
Cdd:COG4372 26 IAALSEQLRKALFELDKLQEELEQ--LREELEQAREELEQLEEELEQARSELEQLE----EELEELNEQLQAAQAELAQA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 265 NQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVEQAievltrsSLEVELAAKEREIAQLVEDVQRLQASLTKLREN 344
Cdd:COG4372 100 QEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIA-------ELQSEIAEREEELKELEEQLESLQEELAALEQE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 345 -----SASQISQLEQQLSAKNSTLKQLEEKLKGQADYEEVKKELNILKSMEFAPSEGAGTQDAAKPLEVLLMEKNRSLQS 419
Cdd:COG4372 173 lqalsEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELL 252
|
....*..
gi 1622917383 420 ENAALRI 426
Cdd:COG4372 253 EEVILKE 259
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
210-484 |
9.39e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.91 E-value: 9.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 210 STTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEettaKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSL 289
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNE----LQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 290 Q-------LASQIQKAPDVE------QAIEVLTRSSLEV--ELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQ 354
Cdd:COG3883 96 YrsggsvsYLDVLLGSESFSdfldrlSALSKIADADADLleELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 355 QLSAKNSTLKQLEEKlkgQADYEEVKKELNilKSMEFAPSEGAGTQDAAKPLEVLLMEKNRSLQSENAALRISNSDLSGS 434
Cdd:COG3883 176 QQAEQEALLAQLSAE---EAAAEAQLAELE--AELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAG 250
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1622917383 435 ARRKGKDQPESRRPGSLPAPPPSQLPRNPGEQASNTNGTHQFSPAGLSQD 484
Cdd:COG3883 251 AAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAAS 300
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
137-433 |
1.30e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 53.44 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 137 ETENQKLRETLEEYNKEFAEVKNQEVTIKALK-EKIREYEQTLKNQAETIALEKEQklqNDFAEKERKLQETQMSTTSKL 215
Cdd:pfam02463 218 KLELEEEYLLYLDYLKLNEERIDLLQELLRDEqEEIESSKQEIEKEEEKLAQVLKE---NKEEEKEKKLQEEELKLLAKE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 216 EEaehkVQSLQTALEKTRTELFDLKTKYDEETTAKAD-EIEMIMTD-LERANQRAEV-AQREAETLREQLSSAN--HSLQ 290
Cdd:pfam02463 295 EE----ELKSELLKLERRKVDDEEKLKESEKEKKKAEkELKKEKEEiEELEKELKELeIKREAEEEEEEELEKLqeKLEQ 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 291 LASQIQKAPDVEQAIEVLTRSSLEVELAAKERE--IAQLVEDVQRLQASLTKLRENSAS------QISQLEQQLSAKNST 362
Cdd:pfam02463 371 LEEELLAKKKLESERLSSAAKLKEEELELKSEEekEAQLLLELARQLEDLLKEEKKEELeileeeEESIELKQGKLTEEK 450
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622917383 363 LKQLEEKLKGQADYEEVKKELNILKSMEFAPSEGAGTQDAAKPLEVLLMEKNRSLQSENAALRISNSDLSG 433
Cdd:pfam02463 451 EELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVG 521
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
141-367 |
2.32e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.61 E-value: 2.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 141 QKLRETLEEYnkefaevknqevtiKALKEKIREYEQtlknQAETIALEKEQKLQNDFAEKERKLQEtqmsttsKLEEAEH 220
Cdd:COG4913 255 EPIRELAERY--------------AAARERLAELEY----LRAALRLWFAQRRLELLEAELEELRA-------ELARLEA 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 221 KVQSLQTALEKTRTELFDLKTKYDEettAKADEIEmimtDLERANQRAEVAQREAETLREQLSSANHSLQLAsqiqkAPD 300
Cdd:COG4913 310 ELERLEARLDALREELDELEAQIRG---NGGDRLE----QLEREIERLERELEERERRRARLEALLAALGLP-----LPA 377
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622917383 301 VEQaievltrsslevELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLE 367
Cdd:COG4913 378 SAE------------EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
133-430 |
2.35e-06 |
|
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: 52.75 E-value: 2.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 133 LHDIETENQKLRETLEEYNKEFAevKNQEVTI--------KALKEKIREYEQTLKNqAETIALEKEQKLQNDFAEKERKL 204
Cdd:TIGR01612 988 LNDYEAKNNELIKYFNDLKANLG--KNKENMLyhqfdekeKATNDIEQKIEDANKN-IPNIEIAIHTSIYNIIDEIEKEI 1064
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 205 -QETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKydEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQls 283
Cdd:TIGR01612 1065 gKNIELLNKEILEEAEINITNFNEIKEKLKHYNFDDFGK--EENIKYADEINKIKDDIKNLDQKIDHHIKALEEIKKK-- 1140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 284 SANHSLQLASQIQKAPDVeqAIEVLTRSSLEvELAAKEREIAQLVEDVQRLQASLTKLrensASQISQLEQQLSA----K 359
Cdd:TIGR01612 1141 SENYIDEIKAQINDLEDV--ADKAISNDDPE-EIEKKIENIVTKIDKKKNIYDEIKKL----LNEIAEIEKDKTSleevK 1213
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622917383 360 NSTL---KQLEEKLKGQADyEEVKKELNILKSMEfAPSEGAGTQDAAKPLEVLLMEKNRSLQSENAALRISNSD 430
Cdd:TIGR01612 1214 GINLsygKNLGKLFLEKID-EEKKKSEHMIKAME-AYIEDLDEIKEKSPEIENEMGIEMDIKAEMETFNISHDD 1285
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
131-333 |
2.40e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.61 E-value: 2.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 131 QRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKNQAETIALekeQKLQNDFAEKERKLQETQmS 210
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAE---LDALQERREALQRLAEYSWDEIDV---ASAEREIAELEAELERLD-A 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 211 TTSKLEEAEHKVQSLQTALEKTRTELFDLKTKY---DEETTAKADEIEMIMTDLERANQRAEVAQRE-AETLREQLSSAN 286
Cdd:COG4913 683 SSDDLAALEEQLEELEAELEELEEELDELKGEIgrlEKELEQAEEELDELQDRLEAAEDLARLELRAlLEERFAAALGDA 762
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1622917383 287 HSLQLASQIQKApdveqaievltRSSLEVELAAKEREIAQLVEDVQR 333
Cdd:COG4913 763 VERELRENLEER-----------IDALRARLNRAEEELERAMRAFNR 798
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
37-390 |
2.54e-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: 52.42 E-value: 2.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 37 ELDATATVLANRQDESEQSRKRLIEqsrefkKNTPEDLRKQVAPLLKSFQGeidalskrsKEAEAAFLnvykrlidvpdp 116
Cdd:pfam05483 392 ELEEMTKFKNNKEVELEELKKILAE------DEKLLDEKKQFEKIAEELKG---------KEQELIFL------------ 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 117 vpaldlgqqLQLKVQRLHDIETENQKLRETLEEYNKEFAE---------VKNQEVTIKALKEKIREYEQTLKNQAETIAL 187
Cdd:pfam05483 445 ---------LQAREKEIHDLEIQLTAIKTSEEHYLKEVEDlktelekekLKNIELTAHCDKLLLENKELTQEASDMTLEL 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 188 EKEQK-LQNDFAEKERKLQEtqmsttskLEEAEHKVQSLQTALEKTRTELF----DLKTKYDE-ETTAKADEIEMImtdl 261
Cdd:pfam05483 516 KKHQEdIINCKKQEERMLKQ--------IENLEEKEMNLRDELESVREEFIqkgdEVKCKLDKsEENARSIEYEVL---- 583
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 262 eRANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVEQAIEV-------LTRSSLEVELAAKEREIAQLVEDVQRl 334
Cdd:pfam05483 584 -KKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENkqlnayeIKVNKLELELASAKQKFEEIIDNYQK- 661
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622917383 335 QASLTKLRENS-----------ASQISQLEQQLSA----KNSTLKQLEEKLKGQAD--YEEVKKELNILKSME 390
Cdd:pfam05483 662 EIEDKKISEEKlleevekakaiADEAVKLQKEIDKrcqhKIAEMVALMEKHKHQYDkiIEERDSELGLYKNKE 734
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
72-388 |
3.36e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.69 E-value: 3.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 72 EDLRKQVApLLKSFQGEIDALSKRSKEAEAAFLNVYKRLIDVPDPVPALDLGQQLQLKVQRLHDIETENQKLRETLEEYN 151
Cdd:COG4717 74 KELEEELK-EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 152 KEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQnDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEK 231
Cdd:COG4717 153 ERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQ-DLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 232 TRTELFDLK-----------------------------------------------------TKYDEETTAKADEIEMI- 257
Cdd:COG4717 232 LENELEAAAleerlkearlllliaaallallglggsllsliltiagvlflvlgllallflllAREKASLGKEAEELQALp 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 258 -MTDLERANQRAEVAQ-------------------REAETLREQLSSANHSLQLASQIQK---------APDVEQAIEVL 308
Cdd:COG4717 312 aLEELEEEELEELLAAlglppdlspeellelldriEELQELLREAEELEEELQLEELEQEiaallaeagVEDEEELRAAL 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 309 TRSSLEVELAAKEREI--------------------AQLVEDVQRLQASLTKLREnsasQISQLEQQLSAKNSTLKQLEE 368
Cdd:COG4717 392 EQAEEYQELKEELEELeeqleellgeleellealdeEELEEELEELEEELEELEE----ELEELREELAELEAELEQLEE 467
|
410 420
....*....|....*....|
gi 1622917383 369 klkgQADYEEVKKELNILKS 388
Cdd:COG4717 468 ----DGELAELLQELEELKA 483
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
43-361 |
3.47e-06 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 52.00 E-value: 3.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 43 TVLANRQDESEQSRKRLIE---QSREFK--KNTPEDLRKQVAPLLKSFQGEIDALSKrSKEAEAAFLnvyKRLIDVPDPV 117
Cdd:COG5022 868 TIYLQSAQRVELAERQLQElkiDVKSISslKLVNLELESEIIELKKSLSSDLIENLE-FKTELIARL---KKLLNNIDLE 943
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 118 PALDLGQQLQLKVQRLHdieTENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKN--------QAETIALEK 189
Cdd:COG5022 944 EGPSIEYVKLPELNKLH---EVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAElskqygalQESTKQLKE 1020
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 190 EQK----LQND----FAEKERKLQETQMS---TTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEmiM 258
Cdd:COG5022 1021 LPVevaeLQSAskiiSSESTELSILKPLQklkGLLLLENNQLQARYKALKLRRENSLLDDKQLYQLESTENLLKTIN--V 1098
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 259 TDLERANQRAEVAQREAETLREQLSSANHSLQ----LASQIQKAPDVEQAIEV-------LTRSSLEVELAAKEREIAqL 327
Cdd:COG5022 1099 KDLEVTNRNLVKPANVLQFIVAQMIKLNLLQEiskfLSQLVNTLEPVFQKLSVlqleldgLFWEANLEALPSPPPFAA-L 1177
|
330 340 350
....*....|....*....|....*....|....
gi 1622917383 328 VEDVQRLQASLTKLRENSASQISQLEQQLSAKNS 361
Cdd:COG5022 1178 SEKRLYQSALYDEKSKLSSSEVNDLKNELIALFS 1211
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
33-338 |
4.28e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.61 E-value: 4.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 33 GIKRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPED---LRKQVAPL---LKSFQGEIDALSKRSKEAEAAFLNV 106
Cdd:TIGR02169 248 SLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEqlrVKEKIGELeaeIASLERSIAEKERELEDAEERLAKL 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 107 YKRLIDVPDPVPALDlGQQLQLKVQRlHDIETENQKLREtleEYNKEFAEVKNQEVTIKALKEKIREYEQtlknqaetiA 186
Cdd:TIGR02169 328 EAEIDKLLAEIEELE-REIEEERKRR-DKLTEEYAELKE---ELEDLRAELEEVDKEFAETRDELKDYRE---------K 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 187 LEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALektrtelfdlkTKYDEETTAKADEIEMIMTDLERANQ 266
Cdd:TIGR02169 394 LEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKI-----------NELEEEKEDKALEIKKQEWKLEQLAA 462
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622917383 267 RAEVAQREAETLREQLSSANHSL-QLASQIQKAPDVEQAIEVLTRSSLEVELAAKER------EIAQLVEDVQRLQASL 338
Cdd:TIGR02169 463 DLSKYEQELYDLKEEYDRVEKELsKLQRELAEAEAQARASEERVRGGRAVEEVLKASiqgvhgTVAQLGSVGERYATAI 541
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
225-371 |
5.11e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 50.67 E-value: 5.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 225 LQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLA-SQIQKAPD-VE 302
Cdd:COG4372 4 LGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQArSELEQLEEeLE 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622917383 303 QAIEVLTRSSLEV-----ELAAKEREIAQLVEDVQRLQASLTKL---RENSASQISQLEQQLSAKNSTLKQLEEKLK 371
Cdd:COG4372 84 ELNEQLQAAQAELaqaqeELESLQEEAEELQEELEELQKERQDLeqqRKQLEAQIAELQSEIAEREEELKELEEQLE 160
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
60-368 |
6.00e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.17 E-value: 6.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 60 IEQSREFKKntpEDLRKQvaplLKSFQGEIDALSKRSKEAEAAfLNVYKRLIDVpdpvpaLDLGQQLQLKVQRLHDIETE 139
Cdd:COG3206 162 LEQNLELRR---EEARKA----LEFLEEQLPELRKELEEAEAA-LEEFRQKNGL------VDLSEEAKLLLQQLSELESQ 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 140 NQKLRETLEEynkefaevknQEVTIKALKEKIREYEQTLKNQAETIALekeQKLQNDFAEKERKLQETQmsttSKLEEAE 219
Cdd:COG3206 228 LAEARAELAE----------AEARLAALRAQLGSGPDALPELLQSPVI---QQLRAQLAELEAELAELS----ARYTPNH 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 220 HKVQSLQTALEKTRTELfdlktkydeettakADEIEMIMTDLEranQRAEVAQREAETLREQLSsanhslQLASQIQKAP 299
Cdd:COG3206 291 PDVIALRAQIAALRAQL--------------QQEAQRILASLE---AELEALQAREASLQAQLA------QLEARLAELP 347
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622917383 300 dveqaievltrsslevelaAKEREIAQLVEDVQRLQASLTKLREnsasQISQLEQQLSAKNSTLKQLEE 368
Cdd:COG3206 348 -------------------ELEAELRRLEREVEVARELYESLLQ----RLEEARLAEALTVGNVRVIDP 393
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
35-382 |
7.91e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 7.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 35 KRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLRKqvAPLLKSFQGE---IDALSKRSKEAEAAflNVYKRLI 111
Cdd:PTZ00121 1365 KAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKK--ADELKKAAAAkkkADEAKKKAEEKKKA--DEAKKKA 1440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 112 DVPDPVPALDLGQQLQLKVQRLHDIETENQKLRETLE--EYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEK 189
Cdd:PTZ00121 1441 EEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKkaEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEE 1520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 190 EQKLQN-DFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTElfdlKTKYDEETTAKADEIEMIMTDLE--RANQ 266
Cdd:PTZ00121 1521 AKKADEaKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAE----EAKKAEEDKNMALRKAEEAKKAEeaRIEE 1596
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 267 RAEVAQREAETLREQLSSANHSLQLASQIQKAPDVEQAIEVLTRSslEVELAAKEREIAQLVEDVQRLQASLTKLRENSA 346
Cdd:PTZ00121 1597 VMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKK--EAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK 1674
|
330 340 350
....*....|....*....|....*....|....*.
gi 1622917383 347 SQISQLEQQLSAKNSTLKQLEEKLKGQADYEEVKKE 382
Cdd:PTZ00121 1675 KKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKK 1710
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
119-384 |
1.01e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.34 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 119 ALDLGQQLQLKVQRLHDIEtenqklrETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLknQAETIALEKEQKLQNDFA 198
Cdd:PRK04863 288 ALELRRELYTSRRQLAAEQ-------YRLVEMARELAELNEAESDLEQDYQAASDHLNLV--QTALRQQEKIERYQADLE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 199 EKERKLQETQMST---TSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTaKADEIEMIMTDLERANQ--------- 266
Cdd:PRK04863 359 ELEERLEEQNEVVeeaDEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQT-RAIQYQQAVQALERAKQlcglpdlta 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 267 -----RAEVAQREAETLREQLSSANHSLQLASQIQKApdVEQAIEVLTRSSLEVelaakEREIAQlvedvQRLQASLTKL 341
Cdd:PRK04863 438 dnaedWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQ--FEQAYQLVRKIAGEV-----SRSEAW-----DVARELLRRL 505
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1622917383 342 RE--NSASQISQLEQQLSAknstlkqLEEKLKGQADYEEVKKELN 384
Cdd:PRK04863 506 REqrHLAEQLQQLRMRLSE-------LEQRLRQQQRAERLLAEFC 543
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
86-382 |
1.01e-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: 50.21 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 86 QGEIDALSKRSKEAEAAFLNVYKRLIDVPDPVPAL-----DLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQ 160
Cdd:pfam10174 344 QTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLageirDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKER 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 161 evtIKALKEKIREYEQTLKNQAETIAlEKE---QKLQNDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELF 237
Cdd:pfam10174 424 ---VKSLQTDSSNTDTALTTLEEALS-EKEriiERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLI 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 238 DLKtkydEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANhslQLASQIQKAPDVEQAIevltrSSLEVEL 317
Cdd:pfam10174 500 DLK----EHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAH---NAEEAVRTNPEINDRI-----RLLEQEV 567
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622917383 318 AAKEREIAQLVEDVQRLQASLtKLRENSAS----QISQLE---------QQLSAKNSTLKQLEEKLKGQADYEEVKKE 382
Cdd:pfam10174 568 ARYKEESGKAQAEVERLLGIL-REVENEKNdkdkKIAELEsltlrqmkeQNKKVANIKHGQQEMKKKGAQLLEEARRR 644
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
80-385 |
1.21e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 50.30 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 80 PLLKSFQGEIDALSKRsKEAEAAFLNVYKRLIDvpdpvpALDLGQQLQlkvqrlhDIETENQKLRETLEEYNKEFAEVKN 159
Cdd:PRK11281 36 PTEADVQAQLDALNKQ-KLLEAEDKLVQQDLEQ------TLALLDKID-------RQKEETEQLKQQLAQAPAKLRQAQA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 160 QevtIKALKEKIreyEQTLKNQAETIALEKeqkLQNDFAEKERKLQETQmsttSKLEEAEHKVQSLQTALEKTRTELFdl 239
Cdd:PRK11281 102 E---LEALKDDN---DEETRETLSTLSLRQ---LESRLAQTLDQLQNAQ----NDLAEYNSQLVSLQTQPERAQAALY-- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 240 ktkydeettakadeiemimtdlerANQraevaQREAEtLREQLSSANHSlqlasqiQKAPDVEQaievltRSSLEVELAA 319
Cdd:PRK11281 167 ------------------------ANS-----QRLQQ-IRNLLKGGKVG-------GKALRPSQ------RVLLQAEQAL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 320 KEREIA---QLVEDVQRLQASLTKLRENSASQISQLEQQL-------SAKNstLKQLEEKLKGQADYEE---------VK 380
Cdd:PRK11281 204 LNAQNDlqrKSLEGNTQLQDLLQKQRDYLTARIQRLEHQLqllqeaiNSKR--LTLSEKTVQEAQSQDEaariqanplVA 281
|
....*
gi 1622917383 381 KELNI 385
Cdd:PRK11281 282 QELEI 286
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
122-459 |
1.27e-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: 49.82 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 122 LGQQLQLKVQRLHDIETENQKLRETLEEynKEfaevknqevtikALKEKIREYEQTLKNQAETIALEKEQkLQNDFAEKE 201
Cdd:pfam10174 329 LKESLTAKEQRAAILQTEVDALRLRLEE--KE------------SFLNKKTKQLQDLTEEKSTLAGEIRD-LKDMLDVKE 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 202 RK----------LQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLktkydEETTAKADE-IEMIMTDLERANQ--RA 268
Cdd:pfam10174 394 RKinvlqkkienLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTL-----EEALSEKERiIERLKEQREREDRerLE 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 269 EVAQ--REAETLREQLSSANhsLQLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIA--QLVEDVQRLQASLTKLREN 344
Cdd:pfam10174 469 ELESlkKENKDLKEKVSALQ--PELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAveQKKEECSKLENQLKKAHNA 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 345 S---------ASQISQLEQQLSAKNstlkqlEEKLKGQAdyeEVKKELNILKSMEfapsegagTQDAAKPLEVLLMEKNR 415
Cdd:pfam10174 547 EeavrtnpeiNDRIRLLEQEVARYK------EESGKAQA---EVERLLGILREVE--------NEKNDKDKKIAELESLT 609
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1622917383 416 SLQSENAALRISN-SDLSGSARRKGKDQ-PESRRPGSLPAPPPSQL 459
Cdd:pfam10174 610 LRQMKEQNKKVANiKHGQQEMKKKGAQLlEEARRREDNLADNSQQL 655
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
67-374 |
1.38e-05 |
|
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: 49.84 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 67 KKNTPEDLRKQVAPLLkSFQGEIDALSKRSKEAEAAFLNVYKRLIDVPDPVPALDLGQQ-------LQLKVQRLH----- 134
Cdd:pfam12128 191 KEGKFRDVKSMIVAIL-EDDGVVPPKSRLNRQQVEHWIRDIQAIAGIMKIRPEFTKLQQefntlesAELRLSHLHfgyks 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 135 ---DIETENQKLRETLEEYNKEFAEVKNQevtikaLKEKIREYEQTLKNQAETIALEKEQ---------KLQNDFAEKER 202
Cdd:pfam12128 270 detLIASRQEERQETSAELNQLLRTLDDQ------WKEKRDELNGELSAADAAVAKDRSElealedqhgAFLDADIETAA 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 203 KLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETtakADEIEMIMTDLE-----RANQRAE---VAQRE 274
Cdd:pfam12128 344 ADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQN---NRDIAGIKDKLAkireaRDRQLAVaedDLQAL 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 275 AETLREQLSSANHSL-----QLAS-------QIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQL-VEDVQRLQASLTKL 341
Cdd:pfam12128 421 ESELREQLEAGKLEFneeeyRLKSrlgelklRLNQATATPELLLQLENFDERIERAREEQEAANAeVERLQSELRQARKR 500
|
330 340 350
....*....|....*....|....*....|...
gi 1622917383 342 RENSASQISQLEQQLSAKNSTLKQLEEKLKGQA 374
Cdd:pfam12128 501 RDQASEALRQASRRLEERQSALDELELQLFPQA 533
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
47-282 |
1.54e-05 |
|
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: 50.06 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 47 NRQDESEQSRKRLIEQSREFKKNTpEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLNVYKRLIDVPDPVPalDLGQQL 126
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEELAEA-EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE--SLERRI 833
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 127 QLKVQRLHDIETENQKLRETLEEYNKEFAE-VKNQEVTIKALKEKIREYEQtlKNQAETIALEKEQKLQNDFAEKERKLQ 205
Cdd:TIGR02168 834 AATERRLEDLEEQIEELSEDIESLAAEIEElEELIEELESELEALLNERAS--LEEALALLRSELEELSEELRELESKRS 911
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622917383 206 ETQmsttSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETtakADEIEMIMTDLERANQRAEVAQREAETLREQL 282
Cdd:TIGR02168 912 ELR----RELEELREKLAQLELRLEGLEVRIDNLQERLSEEY---SLTLEEAEALENKIEDDEEEARRRLKRLENKI 981
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
34-423 |
2.03e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.75 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 34 IKRELDATATVLANRQDESEQSRKRLIEQSREFK-KNTPEDLRKQVApllksfQGEIDALSKRSKEAEAAfLNVYKRLID 112
Cdd:PTZ00121 1254 IRKFEEARMAHFARRQAAIKAEEARKADELKKAEeKKKADEAKKAEE------KKKADEAKKKAEEAKKA-DEAKKKAEE 1326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 113 VPDPVPALDLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKA--LKEKIREYEQT---------LKNQ 181
Cdd:PTZ00121 1327 AKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKAdaAKKKAEEKKKAdeakkkaeeDKKK 1406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 182 AETIALEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTElfDLKTKYDEETtaKADEIEMIMTDL 261
Cdd:PTZ00121 1407 ADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAE--EAKKKAEEAK--KADEAKKKAEEA 1482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 262 ERANQ---RAEVAQREAETLREQLSSANHSLQL--------------------ASQIQKAPDVEQAIEVltRSSLEVELA 318
Cdd:PTZ00121 1483 KKADEakkKAEEAKKKADEAKKAAEAKKKADEAkkaeeakkadeakkaeeakkADEAKKAEEKKKADEL--KKAEELKKA 1560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 319 AKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKLKGQAD----YEEVKKELNILKSMEFAPS 394
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEakikAEELKKAEEEKKKVEQLKK 1640
|
410 420
....*....|....*....|....*....
gi 1622917383 395 EGAgtQDAAKPLEVLLMEKNRSLQSENAA 423
Cdd:PTZ00121 1641 KEA--EEKKKAEELKKAEEENKIKAAEEA 1667
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
45-251 |
2.40e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.86 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 45 LANRQDESEQSRKRLieqsREFKKNT----PEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLNVYKRLIDVPDPVPAL 120
Cdd:COG3206 184 LPELRKELEEAEAAL----EEFRQKNglvdLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 121 DLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKNQAET---IALEKEQKLQNDF 197
Cdd:COG3206 260 LQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQ---IAALRAQLQQEAQRILASLEAeleALQAREASLQAQL 336
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1622917383 198 AEKERKLQETQmSTTSKLEEAEHKVQSLQTALEktrtelfDLKTKYDEETTAKA 251
Cdd:COG3206 337 AQLEARLAELP-ELEAELRRLEREVEVARELYE-------SLLQRLEEARLAEA 382
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
35-260 |
2.45e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.37 E-value: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 35 KRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEaaflnvykrlidvP 114
Cdd:PTZ00121 1592 ARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEE-------------E 1658
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 115 DPVPALDLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKnqAETIALEKEQKLQ 194
Cdd:PTZ00121 1659 NKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKK--AEEENKIKAEEAK 1736
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622917383 195 NDFAEKERKLQETQmsttsKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTD 260
Cdd:PTZ00121 1737 KEAEEDKKKAEEAK-----KDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVD 1797
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
35-387 |
2.55e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.16 E-value: 2.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 35 KRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLNVYKRLIDVP 114
Cdd:COG1196 428 EALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFL 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 115 DPVPALDLGQQLQLKVQRLHDIETENQKLRETLEEynkefaevknqeVTIKALKEKIREYEQTLknqAETIALEKEQKLQ 194
Cdd:COG1196 508 EGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEA------------ALAAALQNIVVEDDEVA---AAAIEYLKAAKAG 572
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 195 NDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQRE 274
Cdd:COG1196 573 RATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLE 652
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 275 AETLREQLSSANHS-------LQLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSAS 347
Cdd:COG1196 653 GEGGSAGGSLTGGSrrellaaLLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEA 732
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1622917383 348 QISQ-LEQQLSAKNSTLKQLEEKLKGQADYEEVKKELNILK 387
Cdd:COG1196 733 EREElLEELLEEEELLEEEALEELPEPPDLEELERELERLE 773
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
133-392 |
2.63e-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: 49.05 E-value: 2.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 133 LHDIETENQKLRET----LEEYNKEFAEVKNQEVTIKALKEKIREYEQTL-KNQAETIALE-KEQKLQNDFAEKERKLQE 206
Cdd:pfam10174 249 IRDLEDEVQMLKTNgllhTEDREEEIKQMEVYKSHSKFMKNKIDQLKQELsKKESELLALQtKLETLTNQNSDCKQHIEV 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 207 TQMSTTSKLEEA---EHKVQSLQTALEKTRTeLFDLKTKY----DEETTAKADEIEMIMTDLERANQRAEVAQREAETLR 279
Cdd:pfam10174 329 LKESLTAKEQRAailQTEVDALRLRLEEKES-FLNKKTKQlqdlTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQ 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 280 EQLSSANHSLQLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQ-------ASLTKLRENSASQISQL 352
Cdd:pfam10174 408 EQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDrerleelESLKKENKDLKEKVSAL 487
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1622917383 353 EQQLSAKNSTLKQLEEKLKGQADyEEVKKElNILKSMEFA 392
Cdd:pfam10174 488 QPELTEKESSLIDLKEHASSLAS-SGLKKD-SKLKSLEIA 525
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
124-378 |
2.73e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 49.02 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 124 QQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVknqevtikaLKEKIREYEQTlknQAETIALEKEQKLQNDFAEKERK 203
Cdd:pfam01576 5 EEMQAKEEELQKVKERQQKAESELKELEKKHQQL---------CEEKNALQEQL---QAETELCAEAEEMRARLAARKQE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 204 LQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEE-------------TTAKADEIEMIMTDLERANQRaev 270
Cdd:pfam01576 73 LEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEeaarqklqlekvtTEAKIKKLEEDILLLEDQNSK--- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 271 AQREAETLREQLSsaNHSLQLASQIQKA--------------PDVEQAI--EVLTRSSLEVELAAKEREIAQLVEDVQRL 334
Cdd:pfam01576 150 LSKERKLLEERIS--EFTSNLAEEEEKAkslsklknkheamiSDLEERLkkEEKGRQELEKAKRKLEGESTDLQEQIAEL 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1622917383 335 QASLTKLR-------ENSASQISQLEQQLSAKNSTLKQLEEKLKGQADYEE 378
Cdd:pfam01576 228 QAQIAELRaqlakkeEELQAALARLEEETAQKNNALKKIRELEAQISELQE 278
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
140-367 |
2.97e-05 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 48.59 E-value: 2.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 140 NQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQA-ETIALEKEQKLQNDFAEKERKLQETQMSTTSKLEEA 218
Cdd:pfam07111 58 SQALSQQAELISRQLQELRRLEEEVRLLRETSLQQKMRLEAQAmELDALAVAEKAGQAEAEGLRAALAGAEMVRKNLEEG 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 219 EHK-VQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLE--RANQRAE--VAQREAETLREQLSSANHSLQ--- 290
Cdd:pfam07111 138 SQReLEEIQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLEtkRAGEAKQlaEAQKEAELLRKQLSKTQEELEaqv 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 291 -LASQIQKAPDvEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQAS--LTKLRENSASQISQL-EQQLSAKNSTLKQL 366
Cdd:pfam07111 218 tLVESLRKYVG-EQVPPEVHSQTWELERQELLDTMQHLQEDRADLQATveLLQVRVQSLTHMLALqEEELTRKIQPSDSL 296
|
.
gi 1622917383 367 E 367
Cdd:pfam07111 297 E 297
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
136-444 |
3.17e-05 |
|
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: 48.58 E-value: 3.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 136 IETENQKLRETLEeYNKEFAEVKNQEVTIKalkekiREYEQTL-KNQAETIALEKEQKLQndfAEKERKLQETqmsttsk 214
Cdd:pfam05557 12 SQLQNEKKQMELE-HKRARIELEKKASALK------RQLDRESdRNQELQKRIRLLEKRE---AEAEEALREQ------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 215 LEEAEHKVQSLQTALEKTRtELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQL----------SS 284
Cdd:pfam05557 75 AELNRLKKKYLEALNKKLN-EKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLdllkakaseaEQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 285 ANHSLQ-----LASQIQKAPDVEQAIEVLTRSSLEVELAAKERE-IAQLVEDVQRLQASLTKLRENSASqISQLEQQLSA 358
Cdd:pfam05557 154 LRQNLEkqqssLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELArIPELEKELERLREHNKHLNENIEN-KLLLKEEVED 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 359 KNSTLKQlEEKLKGQADYEEVKKELNILKSMEFAPSEGAGTQDAAKPleVLLMEKNRSLQSENAALRISNSDLSGSARRK 438
Cdd:pfam05557 233 LKRKLER-EEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSP--EDLSRRIEQLQQREIVLKEENSSLTSSARQL 309
|
....*.
gi 1622917383 439 GKDQPE 444
Cdd:pfam05557 310 EKARRE 315
|
|
| COG5576 |
COG5576 |
Homeodomain-containing transcription factor [Transcription]; |
1270-1355 |
3.77e-05 |
|
Homeodomain-containing transcription factor [Transcription];
Pssm-ID: 227863 [Multi-domain] Cd Length: 156 Bit Score: 45.51 E-value: 3.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 1270 KKPRVVLAPEEKEALKRAYQQKPYPSPKTIEDLATQLNLKTSTVINWFHNYRSRIRRelfieeiqagsQGQAGASDSPSA 1349
Cdd:COG5576 52 KSKRRRTTDEQLMVLEREFEINPYPSSITRIKLSLLLNMPPKSVQIWFQNKRAKEKK-----------KRSGKVEQRPGE 120
|
....*.
gi 1622917383 1350 RSGRAA 1355
Cdd:COG5576 121 EEADLA 126
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
135-447 |
4.02e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 4.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 135 DIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQT-LKNQAETIALEKEQKLqndfAEKERKLQETQMSTTS 213
Cdd:PTZ00121 1040 DVLKEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDaKEDNRADEATEEAFGK----AEEAKKTETGKAEEAR 1115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 214 KLEEAEHKVQSLQTALEKTRTElfDLKtKYDEETTAKADEIEMIMTDLERAnQRAEVAQReaetlreqlssanhslqlAS 293
Cdd:PTZ00121 1116 KAEEAKKKAEDARKAEEARKAE--DAR-KAEEARKAEDAKRVEIARKAEDA-RKAEEARK------------------AE 1173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 294 QIQKAPDVEQAIEVltRSSLEVELAAKEREI--AQLVEDVQRLQASLTKLRENSASQISQLEQqlsaknsTLKQLEEKLK 371
Cdd:PTZ00121 1174 DAKKAEAARKAEEV--RKAEELRKAEDARKAeaARKAEEERKAEEARKAEDAKKAEAVKKAEE-------AKKDAEEAKK 1244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622917383 372 GqadyEEVKKELNILKSMEFAPSEGAGTQDAAKPLEVLLMEKNRSLQSENAALRISNSDLSGSARRKGKDQPESRR 447
Cdd:PTZ00121 1245 A----EEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKK 1316
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
86-372 |
4.08e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.41 E-value: 4.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 86 QGEIDALSKRSKEAEAAFLNVYKRLIDVpdpVPALDLGQ----QLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQE 161
Cdd:PRK04863 375 DEQQEENEARAEAAEEEVDELKSQLADY---QQALDVQQtraiQYQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKE 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 162 vtiKALKEKIREYEQTLkNQAETIALEKEQKLQ-----NDFAEKERKlQETQMSTTSKLEEAEHKVQSLQTAlektRTEL 236
Cdd:PRK04863 452 ---QEATEELLSLEQKL-SVAQAAHSQFEQAYQlvrkiAGEVSRSEA-WDVARELLRRLREQRHLAEQLQQL----RMRL 522
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 237 FDLKTKYDEETTAKA-------------DEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSL-QLASQIQK----A 298
Cdd:PRK04863 523 SELEQRLRQQQRAERllaefckrlgknlDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLeQLQARIQRlaarA 602
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 299 PDVEQAIEVLTRSSLEVELAAKERE-IAQLVEDVQRLQASLTKLRENSASQISQLEQQLS-------AKNSTLKQLEEKL 370
Cdd:PRK04863 603 PAWLAAQDALARLREQSGEEFEDSQdVTEYMQQLLERERELTVERDELAARKQALDEEIErlsqpggSEDPRLNALAERF 682
|
..
gi 1622917383 371 KG 372
Cdd:PRK04863 683 GG 684
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
122-371 |
5.22e-05 |
|
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: 47.38 E-value: 5.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 122 LGQQLQLkvqrLHDIETENQKLRETLEEYNKEfaevknqevTIKALKEKIREYEQTLKNQAETIAL------EKEQKLQN 195
Cdd:pfam04108 40 LSVQLAN----LEKVREGLEKVLNELKKDFKQ---------LLKDLDAALERLEETLDKLRNTPVEpalppgEEKQKTLL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 196 DFAEkERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKtKYDEETTAKADEIEMIMTDLERANQRAEvaqrEA 275
Cdd:pfam04108 107 DFID-EDSVEILRDALKELIDELQAAQESLDSDLKRFDDDLRDLQ-KELESLSSPSESISLIPTLLKELESLEE----EM 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 276 ETLREQLssANHsLQLASQIQKAPDVEQA--IEVLTRSSLEV-----ELAAKEREIAQLVEDVQRLQASLTKLRENSAS- 347
Cdd:pfam04108 181 ASLLESL--TNH-YDQCVTAVKLTEGGRAemLEVLENDARELddvvpELQDRLDEMENNYERLQKLLEQKNSLIDELLSa 257
|
250 260
....*....|....*....|....*.
gi 1622917383 348 --QISQLEQQLSAKNSTLKQLEEKLK 371
Cdd:pfam04108 258 lqLIAEIQSRLPEYLAALKEFEERWE 283
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
132-241 |
6.08e-05 |
|
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: 46.93 E-value: 6.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 132 RLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAET---IALEKEQKLQNDFA---EKERKLQ 205
Cdd:smart00787 138 RMKLLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQlkqLEDELEDCDPTELDrakEKLKKLL 217
|
90 100 110
....*....|....*....|....*....|....*.
gi 1622917383 206 ETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKT 241
Cdd:smart00787 218 QEIMIKVKKLEELEEELQELESKIEDLTNKKSELNT 253
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
144-424 |
6.48e-05 |
|
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: 47.73 E-value: 6.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 144 RETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKnqaetiALEK-EQKLQNDFAEKERKLQETQMSTTSKLEEAEHKV 222
Cdd:TIGR00606 237 REIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIK------ALKSrKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNH 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 223 QSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQ---------REAETLREQLSSANHSLQLAS 293
Cdd:TIGR00606 311 QRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQehirardslIQSLATRLELDGFERGPFSER 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 294 QIQKAPDVE---QAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKL 370
Cdd:TIGR00606 391 QIKNFHTLVierQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSS 470
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622917383 371 KG--QADYEEVKKELNILKSMEFAPSEGAGTQDAA-KPLEVLLMEKNRSLQSENAAL 424
Cdd:TIGR00606 471 DRilELDQELRKAERELSKAEKNSLTETLKKEVKSlQNEKADLDRKLRKLDQEMEQL 527
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
124-388 |
7.47e-05 |
|
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: 47.32 E-value: 7.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 124 QQLQLKVQRL-HDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIReyeqTLKNQaETIALEKEQKLQND--FAEK 200
Cdd:TIGR04523 36 KQLEKKLKTIkNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIK----DLNDK-LKKNKDKINKLNSDlsKINS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 201 ERKLQETQMSTT----SKLEEAEHKVQSLQ----TALEKTRTELFDLKTKYDEETTakadEIEMIMTDLERANQRAEVAQ 272
Cdd:TIGR04523 111 EIKNDKEQKNKLevelNKLEKQKKENKKNIdkflTEIKKKEKELEKLNNKYNDLKK----QKEELENELNLLEKEKLNIQ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 273 REAETLREQLSSANHSL-QLASQIQKAPDVEQAIEVL--TRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQI 349
Cdd:TIGR04523 187 KNIDKIKNKLLKLELLLsNLKKKIQKNKSLESQISELkkQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIK 266
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1622917383 350 SQLE---QQLSAKNSTLKQLEEKLKgqadyeEVKKELNILKS 388
Cdd:TIGR04523 267 KQLSekqKELEQNNKKIKELEKQLN------QLKSEISDLNN 302
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
123-369 |
8.17e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 47.64 E-value: 8.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 123 GQQLQLKVQRLH-DIETENQKLRE---TLEEYNKEFAEVKNQ----EVTIKALKEKIREYEQTLKNQaETIALEKEQKLQ 194
Cdd:COG3096 342 ALRQQEKIERYQeDLEELTERLEEqeeVVEEAAEQLAEAEARleaaEEEVDSLKSQLADYQQALDVQ-QTRAIQYQQAVQ 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 195 NdFAEKERKLQETQMSttskLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKA--DE----IEMIMTDLER--ANQ 266
Cdd:COG3096 421 A-LEKARALCGLPDLT----PENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRqfEKayelVCKIAGEVERsqAWQ 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 267 RAE-----------VAQReAETLREQLSSANhslQLASQIQKApdVEQAIEVLTRSSLEVELAAK-EREIAQLVEDVQRL 334
Cdd:COG3096 496 TARellrryrsqqaLAQR-LQQLRAQLAELE---QRLRQQQNA--ERLLEEFCQRIGQQLDAAEElEELLAELEAQLEEL 569
|
250 260 270
....*....|....*....|....*....|....*
gi 1622917383 335 QASLTKLREnsasQISQLEQQLSAKNSTLKQLEEK 369
Cdd:COG3096 570 EEQAAEAVE----QRSELRQQLEQLRARIKELAAR 600
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
74-280 |
8.99e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 8.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 74 LRKQVAPLLKSFQgEIDALSKRSKEAEAAFLNVYKR--LIDVPDPVPALDLGQQLQLKVQRLHDIETENQKLR------- 144
Cdd:COG4717 293 LAREKASLGKEAE-ELQALPALEELEEEELEELLAAlgLPPDLSPEELLELLDRIEELQELLREAEELEEELQleeleqe 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 145 --ETLEEYN----KEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIaleKEQKLQNDFAEKERKLQETQMsttsKLEEA 218
Cdd:COG4717 372 iaALLAEAGvedeEELRAALEQAEEYQELKEELEELEEQLEELLGEL---EELLEALDEEELEEELEELEE----ELEEL 444
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622917383 219 EHKVQSLQTALEKTRTELFDLKTkyDEETTAKADEIEMIMTDLERANQRAEVAQREAETLRE 280
Cdd:COG4717 445 EEELEELREELAELEAELEQLEE--DGELAELLQELEELKAELRELAEEWAALKLALELLEE 504
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
68-387 |
9.05e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.20 E-value: 9.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 68 KNTPEDLRKQVAPL------LKSFQGEIDALSK--------------RSKEAEAAFLNVYKRLIDVPDPVPAL----DLG 123
Cdd:PRK01156 172 KDVIDMLRAEISNIdyleekLKSSNLELENIKKqiaddekshsitlkEIERLSIEYNNAMDDYNNLKSALNELssleDMK 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 124 QQLQLKVQ----RLHDIETENQKLRETLEEYNK--EFAEVKNQEVTIKALKEK--IREYEQTLKNQAETIA--------L 187
Cdd:PRK01156 252 NRYESEIKtaesDLSMELEKNNYYKELEERHMKiiNDPVYKNRNYINDYFKYKndIENKKQILSNIDAEINkyhaiikkL 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 188 EKEQKLQNDFAEKERKLQETQmSTTSKLEEAEHKVQSLQTALEKtrtelfdLKTKYDEETTAKADEIEMIMTDLERANQR 267
Cdd:PRK01156 332 SVLQKDYNDYIKKKSRYDDLN-NQILELEGYEMDYNSYLKSIES-------LKKKIEEYSKNIERMSAFISEILKIQEID 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 268 AEVAQREAETLR---EQLSSANHSLQ--LASQIQKAPDVEQAIEVLT---------------------------RSSLEV 315
Cdd:PRK01156 404 PDAIKKELNEINvklQDISSKVSSLNqrIRALRENLDELSRNMEMLNgqsvcpvcgttlgeeksnhiinhynekKSRLEE 483
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622917383 316 ELAAKEREIAQLVEDVQRLQASLTKLR-------ENSASQISQLEQQLSAKNSTLKQLEEKlkgQADYEEVKKELNILK 387
Cdd:PRK01156 484 KIREIEIEVKDIDEKIVDLKKRKEYLEseeinksINEYNKIESARADLEDIKIKINELKDK---HDKYEEIKNRYKSLK 559
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
9-291 |
9.15e-05 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 47.06 E-value: 9.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 9 APQTPVESPTASSKLPQAHWLCSPGIKRELDATATVLANRQDESeqsrkrLIEQSREFKKNTPEDLRKQVAPLLKSFQGE 88
Cdd:pfam09731 200 NLAKQSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLAK------LVDQYKELVASERIVFQQELVSIFPDIIPV 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 89 IDALSKRSKEAEAAFLNVYKRLIDVpdpvpaldLGQQLQ-LKVQRLHDIETENQKLRETL----EEYNKEFAEVKNQE-- 161
Cdd:pfam09731 274 LKEDNLLSNDDLNSLIAHAHREIDQ--------LSKKLAeLKKREEKHIERALEKQKEELdklaEELSARLEEVRAADea 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 162 ---VTIKALKEKIRE-YEQTLKNQAETIALEKEQKLQNDFAEKERKLQETQMsttskleeaehkvQSLQTALEKTRtelf 237
Cdd:pfam09731 346 qlrLEFEREREEIREsYEEKLRTELERQAEAHEEHLKDVLVEQEIELQREFL-------------QDIKEKVEEER---- 408
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622917383 238 DLKTKYDEETTAKADEIEMIMT---DLERANQRAEVAQREAETLREQLSSANHSLQL 291
Cdd:pfam09731 409 AGRLLKLNELLANLKGLEKATSshsEVEDENRKAQQLWLAVEALRSTLEDGSADSRP 465
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
132-424 |
9.44e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 47.42 E-value: 9.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 132 RLHDIETENQKLRETLEEYNKEFAE--VKNQEVTIKALKEKI---REYEQTLKNQAETIalEKEQKLQND-FAEKERKLQ 205
Cdd:pfam15921 246 QLEALKSESQNKIELLLQQHQDRIEqlISEHEVEITGLTEKAssaRSQANSIQSQLEII--QEQARNQNSmYMRQLSDLE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 206 ETQMSTTSKLEEA----EHKVQSLQTALEKTRTELFDLKTKYDE---ETTAKADEIEMIMTDLERANQRAEVAQREAETL 278
Cdd:pfam15921 324 STVSQLRSELREAkrmyEDKIEELEKQLVLANSELTEARTERDQfsqESGNLDDQLQKLLADLHKREKELSLEKEQNKRL 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 279 REQlssanhslqlasqiqkapDVEQAIevlTRSSLEVELAAKEREiaqlvedVQRLQASLTKLRENSAsqiSQLEQQLSA 358
Cdd:pfam15921 404 WDR------------------DTGNSI---TIDHLRRELDDRNME-------VQRLEALLKAMKSECQ---GQMERQMAA 452
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622917383 359 KNSTLKQLEEKLKGQADYEEVKKEL-NILKSMEFAPSEGAGTQDAAKPLEVLLMEKNRSLQSENAAL 424
Cdd:pfam15921 453 IQGKNESLEKVSSLTAQLESTKEMLrKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEI 519
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
29-419 |
1.06e-04 |
|
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: 46.61 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 29 LCSPGIKRELDATatvlanRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLlksfQGEIDALSKRSKEAEAaflnvYK 108
Cdd:pfam05622 53 SGTPGGKKYLLLQ------KQLEQLQEENFRLETARDDYRIKCEELEKEVLEL----QHRNEELTSLAEEAQA-----LK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 109 RLIDVpdpvpaldlgqqLQLKVQRLHDIETENQKLRETLEEYNkefaEVKNQevtIKALKEKIREYEQtlknqaETIALE 188
Cdd:pfam05622 118 DEMDI------------LRESSDKVKKLEATVETYKKKLEDLG----DLRRQ---VKLLEERNAEYMQ------RTLQLE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 189 KEQK----LQNDFAEKERKLQETQ------MSTTSKLE----EAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEI 254
Cdd:pfam05622 173 EELKkanaLRGQLETYKRQVQELHgklseeSKKADKLEfeykKLEEKLEALQKEKERLIIERDTLRETNEELRCAQLQQA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 255 EMIMTD----------------------------LERANQRAEVAQREAE-----TLREQLSSANHSL-----QLASQIQ 296
Cdd:pfam05622 253 ELSQADallspssdpgdnlaaeimpaeireklirLQHENKMLRLGQEGSYrerltELQQLLEDANRRKneletQNRLANQ 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 297 KAPDVEQAIEVLTRSSLEV-----ELAAKEREIAQLVEDVQRLQASLTKLRE-----------NSASQISQLEQQLSAKN 360
Cdd:pfam05622 333 RILELQQQVEELQKALQEQgskaeDSSLLKQKLEEHLEKLHEAQSELQKKKEqieelepkqdsNLAQKIDELQEALRKKD 412
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622917383 361 STLKQLEEKLKgqadyEEVKKELNILKSMEfaPSEGAGTQDAAKPLEVLLMEKNRSLQS 419
Cdd:pfam05622 413 EDMKAMEERYK-----KYVEKAKSVIKTLD--PKQNPASPPEIQALKNQLLEKDKKIEH 464
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
121-390 |
1.25e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 47.04 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 121 DLGQQLQ---------------------LKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLK 179
Cdd:pfam15921 500 DLTASLQekeraieatnaeitklrsrvdLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVG 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 180 NQAET---IALEKEQkLQNDFAEKERKLQETQM---STTSKLEEAEHKVQSLQtaLEKTR-----TELFDLKTKYDEETT 248
Cdd:pfam15921 580 QHGRTagaMQVEKAQ-LEKEINDRRLELQEFKIlkdKKDAKIRELEARVSDLE--LEKVKlvnagSERLRAVKDIKQERD 656
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 249 AKADEIEMIMTDLERANQRAEVAQR-------EAET----LREQLSSANHSLQLASQIQKAPDVEQAIEVLTRSSLEVEL 317
Cdd:pfam15921 657 QLLNEVKTSRNELNSLSEDYEVLKRnfrnkseEMETttnkLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQI 736
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622917383 318 AAKEREIAQLVEDVQRLQASLTKLRENSASqISQLEQQLSAKNSTLKQLEEKLKGqadyeevkkELNILKSME 390
Cdd:pfam15921 737 TAKRGQIDALQSKIQFLEEAMTNANKEKHF-LKEEKNKLSQELSTVATEKNKMAG---------ELEVLRSQE 799
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
235-387 |
1.30e-04 |
|
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: 46.39 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 235 ELFD-LKTKYDEETTAKADEIEMIMTDLERANQRAEV--AQREAETLREQLSSANHSLQlasQIQKapDVEQAIEVLTRS 311
Cdd:pfam06160 45 EKFEeWRKKWDDIVTKSLPDIEELLFEAEELNDKYRFkkAKKALDEIEELLDDIEEDIK---QILE--ELDELLESEEKN 119
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622917383 312 SLEVElaakereiaQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEkLKGQADYEEVKKELNILK 387
Cdd:pfam06160 120 REEVE---------ELKDKYRELRKTLLANRFSYGPAIDELEKQLAEIEEEFSQFEE-LTESGDYLEAREVLEKLE 185
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
213-483 |
1.36e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 213 SKLEEAEHKVQSLQTALEKTRTELFDLktkydeettakADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSL--- 289
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDAL-----------QAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIeer 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 290 -----QLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLK 364
Cdd:COG3883 85 reelgERARALYRSGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 365 QLEEKLKG-QADYEEVKKELNILKsmefapSEGAGTQDAAKPLEVLLMEKNRSLQSENAALRISNSDLSGSARRKGKDQP 443
Cdd:COG3883 165 ELEAAKAElEAQQAEQEALLAQLS------AEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1622917383 444 ESRRPGSLPAPPPSQLPRNPGEQASNTNGTHQFSPAGLSQ 483
Cdd:COG3883 239 AAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAA 278
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
772-958 |
1.41e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 46.86 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 772 STSPMPTVSSYPPLAISLKKPSAAPEAG--ASALPNPPALKKEAQDAPGLDPQGAADCAQGVLR--QVKNEVGRSGAWkd 847
Cdd:PHA03247 269 PETARGATGPPPPPEAAAPNGAAAPPDGvwGAALAGAPLALPAPPDPPPPAPAGDAEEEDDEDGamEVVSPLPRPRQH-- 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 848 hwWSAVQPERRNAASSEEAKAEETGGgkekgsggsgggsqprAERSQLQGPSSSEYWKEWPSAESPYSQSSELSLTGASR 927
Cdd:PHA03247 347 --YPLGFPKRRRPTWTPPSSLEDLSA----------------GRHHPKRASLPTRKRRSARHAATPFARGPGGDDQTRPA 408
|
170 180 190
....*....|....*....|....*....|.
gi 1622917383 928 SETPQNSPLPSSPIVPMSKPTKPSVPPLTPE 958
Cdd:PHA03247 409 APVPASVPTPAPTPVPASAPPPPATPLPSAE 439
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
139-404 |
1.68e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 139 ENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIRE----YEQTLKNQAETIALEKEQKLQNDFAEKERKLQETQMSTTSK 214
Cdd:PTZ00121 1562 EKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEvmklYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKK 1641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 215 LEEAEHKVQSLQtalektrtelfdlktKYDEETTAKADEIEmimTDLERANQRAEVAQREAEtlrEQLSSANHSLQLASQ 294
Cdd:PTZ00121 1642 EAEEKKKAEELK---------------KAEEENKIKAAEEA---KKAEEDKKKAEEAKKAEE---DEKKAAEALKKEAEE 1700
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 295 IQKAPDVEQAIEVLTRSSLEVELAAKEREI----AQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTL-KQLEEK 369
Cdd:PTZ00121 1701 AKKAEELKKKEAEEKKKAEELKKAEEENKIkaeeAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIrKEKEAV 1780
|
250 260 270
....*....|....*....|....*....|....*
gi 1622917383 370 LKGQADYEEVKKELNILKSMEFAPSEGAGTQDAAK 404
Cdd:PTZ00121 1781 IEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGK 1815
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
133-390 |
1.84e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 133 LHDIETENQKLRETLEEYNKEFAEVKNQEVtIKALKEKIREYEQTLKNQAETIALEKEQKlqndfAEKERKLQEtqmstt 212
Cdd:PRK03918 141 LESDESREKVVRQILGLDDYENAYKNLGEV-IKEIKRRIERLEKFIKRTENIEELIKEKE-----KELEEVLRE------ 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 213 skLEEAEHKVQSLQTALEKTRTELFDLKtKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSsanhslQLA 292
Cdd:PRK03918 209 --INEISSELPELREELEKLEKEVKELE-ELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIE------ELE 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 293 SQIQKAPDVEQ-AIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKlrensasQISQLEQQLSAKNSTLKQLEEKLK 371
Cdd:PRK03918 280 EKVKELKELKEkAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEE-------RIKELEEKEERLEELKKKLKELEK 352
|
250
....*....|....*....
gi 1622917383 372 GQADYEEVKKELNILKSME 390
Cdd:PRK03918 353 RLEELEERHELYEEAKAKK 371
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
63-382 |
1.85e-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: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 63 SREFKKNtpEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLNVYKRLIDVPDpvpALDLGQQLQLKVQRLHDIETENQK 142
Cdd:TIGR00618 183 LMEFAKK--KSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLRE---ALQQTQQSHAYLTQKREAQEEQLK 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 143 LRETLEEYNKEFAEVKNQEVTIKALKEKIreyeqTLKNQAETIALEKEQKLQNDFaEKERKLQETQmSTTSKLEEAEHKV 222
Cdd:TIGR00618 258 KQQLLKQLRARIEELRAQEAVLEETQERI-----NRARKAAPLAAHIKAVTQIEQ-QAQRIHTELQ-SKMRSRAKLLMKR 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 223 QSLQtalektrTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAE-----TLREQLSSANHSLQLASQIQK 297
Cdd:TIGR00618 331 AAHV-------KQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLtqhihTLQQQKTTLTQKLQSLCKELD 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 298 APDVEQA---IEVLTRSSLEVELAAKEREI-AQLVEDVQRLQASLTKLRENSASQISQLE--QQLSAKNSTLKQLEEKLK 371
Cdd:TIGR00618 404 ILQREQAtidTRTSAFRDLQGQLAHAKKQQeLQQRYAELCAAAITCTAQCEKLEKIHLQEsaQSLKEREQQLQTKEQIHL 483
|
330
....*....|.
gi 1622917383 372 gqaDYEEVKKE 382
Cdd:TIGR00618 484 ---QETRKKAV 491
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
136-390 |
2.25e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 45.88 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 136 IETENQKLRETLEEYNKEFAEVKNQEVTIKAlkEKIRE-----YEQTLKNQAETIALEKEQKLQNDFAEKERKLQETQMS 210
Cdd:pfam17380 344 MERERELERIRQEERKRELERIRQEEIAMEI--SRMRElerlqMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVE 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 211 TTSKLEEAEHKVQSLQTALEKTRtelfdlktkydeettakADEIEMI-MTDLERANQRAEVAQREAETLREQLssanhsl 289
Cdd:pfam17380 422 MEQIRAEQEEARQREVRRLEEER-----------------AREMERVrLEEQERQQQVERLRQQEEERKRKKL------- 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 290 qlasQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQlvedVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQ--LE 367
Cdd:pfam17380 478 ----ELEKEKRDRKRAEEQRRKILEKELEERKQAMIE----EERKRKLLEKEMEERQKAIYEEERRREAEEERRKQqeME 549
|
250 260
....*....|....*....|...
gi 1622917383 368 EKLKGQADYEEVKKELNILKSME 390
Cdd:pfam17380 550 ERRRIQEQMRKATEERSRLEAME 572
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
35-408 |
2.85e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 45.50 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 35 KRELDATATVLANRQDESEQSRKRLIEQSREFKK---------NTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAF-- 103
Cdd:pfam05557 50 NQELQKRIRLLEKREAEAEEALREQAELNRLKKKylealnkklNEKESQLADAREVISCLKNELSELRRQIQRAELELqs 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 104 ----LNVYKRLIDVPDP--VPALDLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKN--QEV----TIKALKEKI 171
Cdd:pfam05557 130 tnseLEELQERLDLLKAkaSEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNskSELaripELEKELERL 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 172 REYEQTLKNQAETIALEKEQKlqndfAEKERKLqetqmsttSKLEEAEHKVQSLQTALEKTRTELfdlktkYDEETTAKA 251
Cdd:pfam05557 210 REHNKHLNENIENKLLLKEEV-----EDLKRKL--------EREEKYREEAATLELEKEKLEQEL------QSWVKLAQD 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 252 DEIEMIMTDLERAnqRAEVAQREAETLREQLSSANHSlqlASQIQKA-PDVEQAIEVLTRSSLEVELAAKEREiaQLVED 330
Cdd:pfam05557 271 TGLNLRSPEDLSR--RIEQLQQREIVLKEENSSLTSS---ARQLEKArRELEQELAQYLKKIEDLNKKLKRHK--ALVRR 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 331 VQRLQASLTKLRENSASQISQLEQQLSAKNSTlKQLEEKLKGQADY-EEVKKELNILK-SMEFAPSEGAGTQDAAKPLEV 408
Cdd:pfam05557 344 LQRRVLLLTKERDGYRAILESYDKELTMSNYS-PQLLERIEEAEDMtQKMQAHNEEMEaQLSVAEEELGGYKQQAQTLER 422
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
124-432 |
3.89e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 3.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 124 QQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKNQAEtiALEKEQKLQNDFAEKERK 203
Cdd:COG4372 31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEE---LEQARSELEQLEEELEELNE--QLQAAQAELAQAQEELES 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 204 LQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYdEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLS 283
Cdd:COG4372 106 LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEI-AEREEELKELEEQLESLQEELAALEQELQALSEAEAEQA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 284 SANHSLQLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTL 363
Cdd:COG4372 185 LDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELE 264
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622917383 364 KQLEEKLKGQADYEEVKKELNILKSMEFAPSEGAGTQDAAKPLEVLLMEKNRSLQSENAALRISNSDLS 432
Cdd:COG4372 265 LAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALA 333
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
37-387 |
4.33e-04 |
|
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: 45.04 E-value: 4.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 37 ELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLRKqvaplLKSFQGEidalSKRSKEAEAA-------FLNVYKR 109
Cdd:TIGR00606 266 KLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLND-----LYHNHQR----TVREKERELVdcqreleKLNKERR 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 110 LIDVPDPVPALDLGqQLQLKVQRLH------DIETENQKLRETLEEYNKEF---AEVKN-QEVTIKALKEKIREYEQTLK 179
Cdd:TIGR00606 337 LLNQEKTELLVEQG-RLQLQADRHQehirarDSLIQSLATRLELDGFERGPfseRQIKNfHTLVIERQEDEAKTAAQLCA 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 180 NQAETIALEKEQ--KLQNDFAEKERKLQETQMSTTSKLEEAEHKVQSLQT-------------ALEKTRTELFDL----- 239
Cdd:TIGR00606 416 DLQSKERLKQEQadEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQlegssdrileldqELRKAERELSKAeknsl 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 240 -KTKYDEETTAKADEIEMIMTdLERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPD------VEQAIEVLTRSS 312
Cdd:TIGR00606 496 tETLKKEVKSLQNEKADLDRK-LRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSrhsdelTSLLGYFPNKKQ 574
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622917383 313 LEVELAAKEREIAQLVEDVQRLQASLTKLRENSasqiSQLEQQLSAKNSTLKQLEEKLKGQADYEEVKKELNILK 387
Cdd:TIGR00606 575 LEDWLHSKSKEINQTRDRLAKLNKELASLEQNK----NHINNELESKEEQLSSYEDKLFDVCGSQDEESDLERLK 645
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
136-367 |
4.44e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.17 E-value: 4.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 136 IETENQKLRETLEEYNKEFAEVKNQ----EVTIKALKEKIREYEQTLKNQAET-------------IALEKEQKLQNDFA 198
Cdd:pfam01576 690 LEQQVEEMKTQLEELEDELQATEDAklrlEVNMQALKAQFERDLQARDEQGEEkrrqlvkqvreleAELEDERKQRAQAV 769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 199 EKERKLQ------ETQMSTTSK-LEEAEHKVQSLQTALEKTRTELFDLKTKYDE------ETTAKADEIEMIMTDLERAN 265
Cdd:pfam01576 770 AAKKKLEldlkelEAQIDAANKgREEAVKQLKKLQAQMKDLQRELEEARASRDEilaqskESEKKLKNLEAELLQLQEDL 849
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 266 QRAEVAQREAETLREQLSSanhslQLASQIQKapdveqaievltRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRE-- 343
Cdd:pfam01576 850 AASERARRQAQQERDELAD-----EIASGASG------------KSALQDEKRRLEARIAQLEEELEEEQSNTELLNDrl 912
|
250 260
....*....|....*....|....*
gi 1622917383 344 -NSASQISQLEQQLSAKNSTLKQLE 367
Cdd:pfam01576 913 rKSTLQVEQLTTELAAERSTSQKSE 937
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1330-1422 |
4.62e-04 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 44.89 E-value: 4.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 1330 IEEIQAGSQGQAGASDSPSARSGRAAPSSEGDSCDGVEATEGPGSADTEEP-----KSQGEAEREEAPRPAEQTEPPPSG 1404
Cdd:PRK12678 55 IKEARGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAApaaraAAAAAAEAASAPEAAQARERRERG 134
|
90
....*....|....*...
gi 1622917383 1405 TPGPDDARDDDHEGGPAE 1422
Cdd:PRK12678 135 EAARRGAARKAGEGGEQP 152
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
82-284 |
4.92e-04 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 43.48 E-value: 4.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 82 LKSFQGEIDALSKRSKEAEAAFLNVYKRLIDVPDPVPALDlgQQLQLKVQRLHDIETENQKLRETLEEYNKEFAE----V 157
Cdd:pfam00261 3 MQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALN--RRIQLLEEELERTEERLAEALEKLEEAEKAADEsergR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 158 KNQEVTIKALKEKIREYEQTLKnQAETIALEKEQKLqndfAEKERKLQETQMS---TTSKLEEAEHKVQSLQTALEKTRT 234
Cdd:pfam00261 81 KVLENRALKDEEKMEILEAQLK-EAKEIAEEADRKY----EEVARKLVVVEGDlerAEERAELAESKIVELEEELKVVGN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1622917383 235 ELFDLKT---KYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSS 284
Cdd:pfam00261 156 NLKSLEAseeKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDR 208
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
42-368 |
6.03e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 44.12 E-value: 6.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 42 ATVLANRQDESEQSRKRLIeQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLNVYKRLIDVpdpvpald 121
Cdd:pfam07888 29 AELLQNRLEECLQERAELL-QAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEEL-------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 122 lgQQLQLKVQRLHDIETENQklRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIalEKEQKLQNDFAEKE 201
Cdd:pfam07888 100 --EEKYKELSASSEELSEEK--DALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERA--KKAGAQRKEEEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 202 RKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLK----TKYDEETTA--KADEIEMIMTDLERANQRAEVAQREA 275
Cdd:pfam07888 174 KQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQdtitTLTQKLTTAhrKEAENEALLEELRSLQERLNASERKV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 276 ETLREQLSS-------------------ANHSLQLAsQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQA 336
Cdd:pfam07888 254 EGLGEELSSmaaqrdrtqaelhqarlqaAQLTLQLA-DASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEE 332
|
330 340 350
....*....|....*....|....*....|...
gi 1622917383 337 SLTKLRensaSQISQLEQQLS-AKNSTLKQLEE 368
Cdd:pfam07888 333 RLQEER----MEREKLEVELGrEKDCNRVQLSE 361
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
121-370 |
7.35e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 43.37 E-value: 7.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 121 DLGQQLQLKVQRLHDI-ETENQKLRETLEEYNKEFAevkNQEVTIKALKEKIREYEQtlKNQAEtiaLEKEQKLQNDFAE 199
Cdd:pfam00038 36 ELRQKKGAEPSRLYSLyEKEIEDLRRQLDTLTVERA---RLQLELDNLRLAAEDFRQ--KYEDE---LNLRTSAENDLVG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 200 KERKLQETQMSTTskleEAEHKVQSLQTalektrtELFDLKTKYDEETTAKADEIEMIMTDLE-RANQRAEVAQREAEtL 278
Cdd:pfam00038 108 LRKDLDEATLARV----DLEAKIESLKE-------ELAFLKKNHEEEVRELQAQVSDTQVNVEmDAARKLDLTSALAE-I 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 279 REQLSS-ANHSLQLASQIQKApDVEQAIEVLTRSSLEVElAAKErEIAQLVEDVQRLQASLTKLRENSAS---QISQLEQ 354
Cdd:pfam00038 176 RAQYEEiAAKNREEAEEWYQS-KLEELQQAAARNGDALR-SAKE-EITELRRTIQSLEIELQSLKKQKASlerQLAETEE 252
|
250 260
....*....|....*....|
gi 1622917383 355 QLSAK----NSTLKQLEEKL 370
Cdd:pfam00038 253 RYELQladyQELISELEAEL 272
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
77-242 |
7.52e-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: 42.99 E-value: 7.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 77 QVAPLLKSFQGEIDALSKRSKEAEAAFLNVYKRLidvpdpvpaldlgQQLQLKVQRLhdiETENQKLRETLEEYNKEFAE 156
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTEL-------------EDLEKEIKRL---ELEIEEVEARIKKYEEQLGN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 157 VKNQ-EVT-----IKALKEKIREYEQTLKNqaetiALEKEQKLQNDFAEKERKLQETQmsttsklEEAEHKVQSLQTALE 230
Cdd:COG1579 85 VRNNkEYEalqkeIESLKRRISDLEDEILE-----LMERIEELEEELAELEAELAELE-------AELEEKKAELDEELA 152
|
170
....*....|..
gi 1622917383 231 KTRTELFDLKTK 242
Cdd:COG1579 153 ELEAELEELEAE 164
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
147-367 |
7.55e-04 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 43.59 E-value: 7.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 147 LEEYNKEFAEVKNQEVTIKALKEKIreyeqtlknqaetIALEKEQKLQNDFaekerklqETQMSTTSKLEEAEHKVQSLQ 226
Cdd:pfam09787 2 LESAKQELADYKQKAARILQSKEKL-------------IASLKEGSGVEGL--------DSSTALTLELEELRQERDLLR 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 227 TALEKTRTELFDLKTKydeettakadeiemiMTDLEranqraEVAQREAETLREQLSSANHslQLASQIQKAPDVEQAIE 306
Cdd:pfam09787 61 EEIQKLRGQIQQLRTE---------------LQELE------AQQQEEAESSREQLQELEE--QLATERSARREAEAELE 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 307 VLTR--SSLEVELaakEREIAQLVEDVQRLQASLTKLR------ENSASQISQLEQQL------------------SAKN 360
Cdd:pfam09787 118 RLQEelRYLEEEL---RRSKATLQSRIKDREAEIEKLRnqltskSQSSSSQSELENRLhqltetliqkqtmlealsTEKN 194
|
....*..
gi 1622917383 361 STLKQLE 367
Cdd:pfam09787 195 SLVLQLE 201
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
139-236 |
7.63e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 7.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 139 ENQKLRETLEEynkefaEVKNQEVTIKALKEKIREYEQTLKNQAETiaLEKeqklqndfaeKERKLQETQMSTTSKLEEA 218
Cdd:PRK12704 65 EIHKLRNEFEK------ELRERRNELQKLEKRLLQKEENLDRKLEL--LEK----------REEELEKKEKELEQKQQEL 126
|
90
....*....|....*...
gi 1622917383 219 EHKVQSLQTALEKTRTEL 236
Cdd:PRK12704 127 EKKEEELEELIEEQLQEL 144
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
141-372 |
8.52e-04 |
|
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: 44.17 E-value: 8.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 141 QKLRETLEEYnkefAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKE-QKLQNDFAEKERKLQETQMSTTSKLEEAE 219
Cdd:COG3096 495 QTARELLRRY----RSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEfCQRIGQQLDAAEELEELLAELEAQLEELE 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 220 HKVQSLQTALEKTRTELFDLKTKYDEETtakadeiemimtdleranQRAEV---AQREAETLREQLSsanhsLQLASqiq 296
Cdd:COG3096 571 EQAAEAVEQRSELRQQLEQLRARIKELA------------------ARAPAwlaAQDALERLREQSG-----EALAD--- 624
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622917383 297 kAPDVEQAIEvltrsslevELAAKEREIAQLVEDVQRLQASLtklrensASQISQLEQQLSAKNSTLKQLEEKLKG 372
Cdd:COG3096 625 -SQEVTAAMQ---------QLLEREREATVERDELAARKQAL-------ESQIERLSQPGGAEDPRLLALAERLGG 683
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
133-423 |
8.64e-04 |
|
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: 43.94 E-value: 8.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 133 LHDIETENQK-LRETLEEYNKEFAEVKNQEVTIKAlkeKIREYEQTLKNQAETIALEKE--QKLQNDFAEKERKLQEtQM 209
Cdd:pfam05483 65 LKDSDFENSEgLSRLYSKLYKEAEKIKKWKVSIEA---ELKQKENKLQENRKIIEAQRKaiQELQFENEKVSLKLEE-EI 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 210 STTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETtakaDEIEMIMTDLeraNQRAEVAQREAETLREQlsSANHSL 289
Cdd:pfam05483 141 QENKDLIKENNATRHLCNLLKETCARSAEKTKKYEYER----EETRQVYMDL---NNNIEKMILAFEELRVQ--AENARL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 290 QLASQIQKAPDVEQAIEvltrSSLEVELAAKEREIA----QLVEDVQRLQaSLTKLRENSASQISQLEQQLSAKNSTLKQ 365
Cdd:pfam05483 212 EMHFKLKEDHEKIQHLE----EEYKKEINDKEKQVSllliQITEKENKMK-DLTFLLEESRDKANQLEEKTKLQDENLKE 286
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622917383 366 LEEKLKG-QADYEEVKKELNilKSMEFAPSEGAGTQDAAKPLEVLLMEKNRSLQSENAA 423
Cdd:pfam05483 287 LIEKKDHlTKELEDIKMSLQ--RSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKA 343
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
57-281 |
9.21e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 9.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 57 KRLIEQSREFKKNTPEDLRKqvapllksfqgeidalSKRSKEAEAAFLNVYKRLIDVPDPVPALDL--GQQLQLKVQRLH 134
Cdd:PTZ00121 1563 KKKAEEAKKAEEDKNMALRK----------------AEEAKKAEEARIEEVMKLYEEEKKMKAEEAkkAEEAKIKAEELK 1626
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 135 DIETENQK---LRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQNDFAEKERKLQETQMST 211
Cdd:PTZ00121 1627 KAEEEKKKveqLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEE 1706
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622917383 212 TSKLEEAE-HKVQSLQTALEKTRTELFDLKTKyDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQ 281
Cdd:PTZ00121 1707 LKKKEAEEkKKAEELKKAEEENKIKAEEAKKE-AEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKE 1776
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
131-236 |
1.04e-03 |
|
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: 42.20 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 131 QRLHDIETENQKLRETLEE--------------YNKEFAEVKNQEVTIKALKEKIREyeqtLKNQAEtIALEKEQKLQND 196
Cdd:pfam13851 47 KLMSEIQQENKRLTEPLQKaqeeveelrkqlenYEKDKQSLKNLKARLKVLEKELKD----LKWEHE-VLEQRFEKVERE 121
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1622917383 197 FAEKERK----LQETQMSTTSKLEEAEHKVQSLQTALEKTRTEL 236
Cdd:pfam13851 122 RDELYDKfeaaIQDVQQKTGLKNLLLEKKLQALGETLEKKEAQL 165
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
54-390 |
1.07e-03 |
|
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: 43.88 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 54 QSRKRLIEQSREFKKNTPEDLRKQVAPL------LKSFQGEIDALSKRSKEAEAAFLNVYKrlidVPDPVPALDlgqqlQ 127
Cdd:TIGR00606 206 QMELKYLKQYKEKACEIRDQITSKEAQLessreiVKSYENELDPLKNRLKEIEHNLSKIMK----LDNEIKALK-----S 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 128 LKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEvtikalKEKIREYEQTLKN-QAETIALEKEQKLQNdfaeKERKLQE 206
Cdd:TIGR00606 277 RKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNH------QRTVREKERELVDcQRELEKLNKERRLLN----QEKTELL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 207 TQMSTTSkLEEAEHKVQSLQTALEK----TRTELFDLKTKYDEETTAK----------ADEIEMIMTDLERANQRAEVAQ 272
Cdd:TIGR00606 347 VEQGRLQ-LQADRHQEHIRARDSLIqslaTRLELDGFERGPFSERQIKnfhtlvierqEDEAKTAAQLCADLQSKERLKQ 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 273 REAETLREQLSSANHSLQLASQIqkapdVEQAIEVLTRSSLEVE-LAAKEREIAQLVEDVQRLQASLTKLRENSASQiSQ 351
Cdd:TIGR00606 426 EQADEIRDEKKGLGRTIELKKEI-----LEKKQEELKFVIKELQqLEGSSDRILELDQELRKAERELSKAEKNSLTE-TL 499
|
330 340 350
....*....|....*....|....*....|....*....
gi 1622917383 352 LEQQLSAKNSTLKQLEEKLKGQADYEEVKKELNILKSME 390
Cdd:TIGR00606 500 KKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQME 538
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
23-302 |
1.24e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.79 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 23 LPQAHWLCSPGIKRELDAtatvLANRQDESEQSRKRLIEQSREFKKntpedlRKQVAPLLKSFQGEIDALSKRSKEAEAA 102
Cdd:PRK04863 881 LPRLNLLADETLADRVEE----IREQLDEAEEAKRFVQQHGNALAQ------LEPIVSVLQSDPEQFEQLKQDYQQAQQT 950
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 103 FLNVYKRLIDVP------------DPVPALDLGQQLQLKV-QRLHDIETENQKLRETLEEYNKEFAEvKNQEVTikALKE 169
Cdd:PRK04863 951 QRDAKQQAFALTevvqrrahfsyeDAAEMLAKNSDLNEKLrQRLEQAEQERTRAREQLRQAQAQLAQ-YNQVLA--SLKS 1027
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 170 KIREYEQTLKnqaetialEKEQKLQN-----DFAEKERKlqetqMSTTSKLEEAEHKVQSLQTALEKTRTELfdlktkyd 244
Cdd:PRK04863 1028 SYDAKRQMLQ--------ELKQELQDlgvpaDSGAEERA-----RARRDELHARLSANRSRRNQLEKQLTFC-------- 1086
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622917383 245 eettakadEIEMimtdlERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVE 302
Cdd:PRK04863 1087 --------EAEM-----DNLTKKLRKLERDYHEMREQVVNAKAGWCAVLRLVKDNGVE 1131
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
155-373 |
1.27e-03 |
|
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: 42.29 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 155 AEVKNQEVTIKALKEKIREYEQTLKNQAETialekeqklqNDFAEKERKLQEtqmsttsKLEEAEHKVQSLQTALEKTRT 234
Cdd:pfam12795 3 DELEKAKLDEAAKKKLLQDLQQALSLLDKI----------DASKQRAAAYQK-------ALDDAPAELRELRQELAALQA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 235 ELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREA---------ETLREQLSSANHSLQ-LASQIQKAPDVEQA 304
Cdd:pfam12795 66 KAEAAPKEILASLSLEELEQRLLQTSAQLQELQNQLAQLNSqlielqtrpERAQQQLSEARQRLQqIRNRLNGPAPPGEP 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622917383 305 IEVLTRSSLEVELAAKEREIAQLvedvQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKLKGQ 373
Cdd:pfam12795 146 LSEAQRWALQAELAALKAQIDML----EQELLSNNNRQDLLKARRDLLTLRIQRLEQQLQALQELLNEK 210
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
47-390 |
1.32e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 47 NRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEA----------EAAFLNVYKRLIDVPDP 116
Cdd:PTZ00121 1087 NRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDArkaeearkaeDAKRVEIARKAEDARKA 1166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 117 VPALDLGQQLQLKVQRLHDIETENQKLRETLE----EYNKEFAEVKNQEVTIKALKEK----IREYEQTLKNQAETIALE 188
Cdd:PTZ00121 1167 EEARKAEDAKKAEAARKAEEVRKAEELRKAEDarkaEAARKAEEERKAEEARKAEDAKkaeaVKKAEEAKKDAEEAKKAE 1246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 189 KEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELF---DLKTKYDE-----ETTAKADEI------ 254
Cdd:PTZ00121 1247 EERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAkkaEEKKKADEakkkaEEAKKADEAkkkaee 1326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 255 -----EMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASqiQKAPDVEQAIEVLTRSSLEV----ELAAKEREIA 325
Cdd:PTZ00121 1327 akkkaDAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAE--KKKEEAKKKADAAKKKAEEKkkadEAKKKAEEDK 1404
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622917383 326 QLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKLKGQAdyEEVKKELNILKSME 390
Cdd:PTZ00121 1405 KKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKA--EEAKKAEEAKKKAE 1467
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
129-367 |
1.39e-03 |
|
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: 43.30 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 129 KVQRLHDI-ETEnqklrETLEEYNKEFAEVKNQEvtIKALKEKIreyeqtlkNQAEtialekeqklqnDFAEKER--KLQ 205
Cdd:pfam06160 33 KVKKLNLTgETQ-----EKFEEWRKKWDDIVTKS--LPDIEELL--------FEAE------------ELNDKYRfkKAK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 206 ETQMSTTSKLEEAEHKVQSLQTAL-------EKTRTELFDLKTKYDEettakadeiemIMTDLEranqraevAQREA--- 275
Cdd:pfam06160 86 KALDEIEELLDDIEEDIKQILEELdelleseEKNREEVEELKDKYRE-----------LRKTLL--------ANRFSygp 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 276 --ETLREQLSSANHSLQLASQIQKAPDVEQAIEVLtrSSLEVELAAKER---EIAQLVEDVQ-RLQASLTKLRE------ 343
Cdd:pfam06160 147 aiDELEKQLAEIEEEFSQFEELTESGDYLEAREVL--EKLEEETDALEElmeDIPPLYEELKtELPDQLEELKEgyreme 224
|
250 260 270
....*....|....*....|....*....|...
gi 1622917383 344 ---------NSASQISQLEQQLSAKNSTLKQLE 367
Cdd:pfam06160 225 eegyalehlNVDKEIQQLEEQLEENLALLENLE 257
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
139-287 |
1.60e-03 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 41.41 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 139 ENQKLRETLEEynkefaEVKNQEVTIKALKEKIREYEQTLKNQAETIAlEKEQKLQndfaEKERKLQETQMSTTSKLEEA 218
Cdd:pfam12072 61 EIHKLRAEAER------ELKERRNELQRQERRLLQKEETLDRKDESLE-KKEESLE----KKEKELEAQQQQLEEKEEEL 129
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622917383 219 EHKVQSLQTALEK----TRTE----LFD-LKTKYDEETTAKADEIEmimtdlERANQRAEVAQREAETLREQLSSANH 287
Cdd:pfam12072 130 EELIEEQRQELERisglTSEEakeiLLDeVEEELRHEAAVMIKEIE------EEAKEEADKKAKEIIALAIQRCAADH 201
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
712-953 |
1.63e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 43.39 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 712 TAEPAQPSSASGSGNSDDAIRSILQQA---RREMEAQQAALDPA---------LKQAPLSQSDITILTPKLlSTSPMPTv 779
Cdd:PHA03247 2833 SAQPTAPPPPPGPPPPSLPLGGSVAPGgdvRRRPPSRSPAAKPAaparppvrrLARPAVSRSTESFALPPD-QPERPPQ- 2910
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 780 ssyPPLAISLKKPSAAPEAGASALPNPPALKKEAQDAPGLDPQGAAdcaqgvlrqvknevGRSGAWKDHWWSAVQPERRN 859
Cdd:PHA03247 2911 ---PQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAG--------------EPSGAVPQPWLGALVPGRVA 2973
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 860 A--------ASSEEAKAEETGGGKEKGSGGSGGGSQPRAERSQLQGPSSSEYWKEWPSAESPYSQSSELSLTGASRSETP 931
Cdd:PHA03247 2974 VprfrvpqpAPSREAPASSTPPLTGHSLSRVSSWASSLALHEETDPPPVSLKQTLWPPDDTEDSDADSLFDSDSERSDLE 3053
|
250 260
....*....|....*....|..
gi 1622917383 932 QNSPLPSSPIVPMSKPTKPSVP 953
Cdd:PHA03247 3054 ALDPLPPEPHDPFAHEPDPATP 3075
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
129-383 |
1.91e-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: 43.02 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 129 KVQRLH-----------------DIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQ 191
Cdd:COG3096 810 KLQRLHqafsqfvgghlavafapDPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLADE 889
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 192 KLQNDFAEKERKLQETQMSTTS------KLEEAEHKVQSLQT------ALEKTRTELFDLKTKYDEETTA---------- 249
Cdd:COG3096 890 TLADRLEELREELDAAQEAQAFiqqhgkALAQLEPLVAVLQSdpeqfeQLQADYLQAKEQQRRLKQQIFAlsevvqrrph 969
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 250 --KADEIEMIM--TDL-ERANQRAEVAQREAETLREQLSsanhslQLASQiqkapdVEQAIEVLT--RSSLEV---ELAA 319
Cdd:COG3096 970 fsYEDAVGLLGenSDLnEKLRARLEQAEEARREAREQLR------QAQAQ------YSQYNQVLAslKSSRDAkqqTLQE 1037
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622917383 320 KEREIAQL------------VEDVQRLQASLTKLRensaSQISQLEQQLSAKNSTLKQLEEKL-KGQADYEEVKKEL 383
Cdd:COG3096 1038 LEQELEELgvqadaeaeeraRIRRDELHEELSQNR----SRRSQLEKQLTRCEAEMDSLQKRLrKAERDYKQEREQV 1110
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
122-375 |
2.17e-03 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 42.59 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 122 LGQQLQLKVQRLH-DIETENQKLRETLEEYNKEFA-EVKNQEVTIKALKEKIREyeqtLKNQAETIALEKeQKLQNDFAE 199
Cdd:pfam15964 361 LKSELERQKERLEkELASQQEKRAQEKEALRKEMKkEREELGATMLALSQNVAQ----LEAQVEKVTREK-NSLVSQLEE 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 200 KERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQR------ 273
Cdd:pfam15964 436 AQKQLASQEMDVTKVCGEMRYQLNQTKMKKDEAEKEHREYRTKTGRQLEIKDQEIEKLGLELSESKQRLEQAQQdaarar 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 274 -EAETLREQLSSANHSLQLASQ----IQKAPDVEQAIEVLTRSSLEVELAAK-----------ERE-----------IAQ 326
Cdd:pfam15964 516 eECLKLTELLGESEHQLHLTRLekesIQQSFSNEAKAQALQAQQREQELTQKmqqmeaqhdktVNEqyslltsqntfIAK 595
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1622917383 327 LVEDVQRLQASLTKLRENSASQISQLEQQlsakNSTLKQLEEKLKGQAD 375
Cdd:pfam15964 596 LKEECCTLAKKLEEITQKSRSEVEQLSQE----KEYLQDRLEKLQKRNE 640
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
54-390 |
2.20e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 42.65 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 54 QSRKRLIEQSREFKKNTPE---DLRKQVAPLLKSFQGEIdaLSKRSKEAEAAFLNVYKRLIDVPDPVPALD-----LGQQ 125
Cdd:TIGR00618 317 QSKMRSRAKLLMKRAAHVKqqsSIEEQRRLLQTLHSQEI--HIRDAHEVATSIREISCQQHTLTQHIHTLQqqkttLTQK 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 126 LQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQNDFAEKERKLQ 205
Cdd:TIGR00618 395 LQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQ 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 206 ETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSS- 284
Cdd:TIGR00618 475 LQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSe 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 285 ANHSLQLASQIQKAPDVEQAIEVLTRSSLEvelaakerEIAQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLK 364
Cdd:TIGR00618 555 RKQRASLKEQMQEIQQSFSILTQCDNRSKE--------DIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQD 626
|
330 340
....*....|....*....|....*.
gi 1622917383 365 QLEEKLKGQADYEEVKKELNILKSME 390
Cdd:TIGR00618 627 LQDVRLHLQQCSQELALKLTALHALQ 652
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
714-982 |
2.23e-03 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 42.76 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 714 EPAQPSSASGSGNSDDairsILQQARREMEAQQAALDPALKQAPLSQ---SDITILTPKLLSTSPMPTVSSYPPLAiSLK 790
Cdd:PRK10263 276 EEITYTARGVAADPDD----VLFSGNRATQPEYDEYDPLLNGAPITEpvaVAAAATTATQSWAAPVEPVTQTPPVA-SVD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 791 KPSAAPEAGASALPNPPAlkKEAQDAPglDPQGAADCAQGVLRQVknevgrsgAWKDHWWSAVQPERRNAASSEEAKAEE 870
Cdd:PRK10263 351 VPPAQPTVAWQPVPGPQT--GEPVIAP--APEGYPQQSQYAQPAV--------QYNEPLQQPVQPQQPYYAPAAEQPAQQ 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 871 TGGGKEKGSGGSGGGSQPRAER----SQLQGPSSSEYWKEWPSAEsPYSQSSELSLTGASRSETPQNSPLPSSPIVPMSK 946
Cdd:PRK10263 419 PYYAPAPEQPAQQPYYAPAPEQpvagNAWQAEEQQSTFAPQSTYQ-TEQTYQQPAAQEPLYQQPQPVEQQPVVEPEPVVE 497
|
250 260 270
....*....|....*....|....*....|....*.
gi 1622917383 947 PTKPSVPPLtpeqyevYMYQEVDtiELTRQVKEKLA 982
Cdd:PRK10263 498 ETKPARPPL-------YYFEEVE--EKRAREREQLA 524
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
126-305 |
2.25e-03 |
|
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.
Pssm-ID: 293683 [Multi-domain] Cd Length: 228 Bit Score: 41.26 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 126 LQLKVQR---LHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQ---TLKNQAETIALEKEQ---KLQND 196
Cdd:pfam17078 20 LQLTVQSqnlLSKLEIAQQKESKFLENLASLKHENDNLSSMLNRKERRLKDLEDqlsELKNSYEELTESNKQlkkRLENS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 197 FAEKERKLQETQMSTT-------SKLEEAEH---KVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQ 266
Cdd:pfam17078 100 SASETTLEAELERLQIqydalvdSQNEYKDHyqqEINTLQESLEDLKLENEKQLENYQQRISSNDKDIDTKLDSYNNKFK 179
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1622917383 267 RAEVAQREAET-LREQLSSANHSLQLASQIQKAPDVEQAI 305
Cdd:pfam17078 180 NLDNIYVNKNNkLLTKLDSLAQLLDLPSWLNLYPESRNKI 219
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
141-338 |
2.58e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 40.96 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 141 QKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETiALEK-EQKLQNDFAEKERKLQETQMSTTSKLEEAE 219
Cdd:COG1842 33 RDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARL-ALEKgREDLAREALERKAELEAQAEALEAQLAQLE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 220 HKVQSLQTALEKTRTELFDLKTKYDeetTAKAdeiemimtdleranqRAEVAQreaetLREQLSSANHSLQLAS------ 293
Cdd:COG1842 112 EQVEKLKEALRQLESKLEELKAKKD---TLKA---------------RAKAAK-----AQEKVNEALSGIDSDDatsale 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1622917383 294 -----QIQKAPDVEQAIEVLTRSSLEVELAAKEREIAqlVEDV-QRLQASL 338
Cdd:COG1842 169 rmeekIEEMEARAEAAAELAAGDSLDDELAELEADSE--VEDElAALKAKM 217
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
36-383 |
2.73e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.47 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 36 RELDATATVLANRQDESEQSRKRLIEQSR-------EFKKNTPEDLR--KQVAPLLKSFQGEIDALSKRSKEAEAAflnv 106
Cdd:pfam01576 492 RQLEDERNSLQEQLEEEEEAKRNVERQLStlqaqlsDMKKKLEEDAGtlEALEEGKKRLQRELEALTQQLEEKAAA---- 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 107 YKRLidvpdpvpaldlgqqlqlkvqrlhdiETENQKLRETLEEYnkeFAEVKNQEVTIKALKEKIREYEQTLknqAETIA 186
Cdd:pfam01576 568 YDKL--------------------------EKTKNRLQQELDDL---LVDLDHQRQLVSNLEKKQKKFDQML---AEEKA 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 187 LEKEQKLQNDFAEKERKLQETQ-MSTTSKLEEAEHKVQSLQTALEKTRTELFDLktkydeetTAKADEIEMIMTDLERAN 265
Cdd:pfam01576 616 ISARYAEERDRAEAEAREKETRaLSLARALEEALEAKEELERTNKQLRAEMEDL--------VSSKDDVGKNVHELERSK 687
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 266 QRAEvaqREAETLREQLSsanhslQLASQIQKAPDVEQAIEVLT---RSSLEVELAAK----EREIAQLVEDVQRLQASL 338
Cdd:pfam01576 688 RALE---QQVEEMKTQLE------ELEDELQATEDAKLRLEVNMqalKAQFERDLQARdeqgEEKRRQLVKQVRELEAEL 758
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622917383 339 TKLRENSASQIS----------QLEQQLSAKN----STLKQLEeklKGQADYEEVKKEL 383
Cdd:pfam01576 759 EDERKQRAQAVAakkkleldlkELEAQIDAANkgreEAVKQLK---KLQAQMKDLQREL 814
|
|
| iSH2_PIK3R2 |
cd12926 |
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory ... |
122-262 |
2.79e-03 |
|
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory subunit 2, PIK3R2, also called p85beta; PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. They play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation, and apoptosis. They are classified according to their substrate specificity, regulation, and domain structure. Class IA PI3Ks are heterodimers of a p110 catalytic (C) subunit and a p85-related regulatory (R) subunit. The R subunit down-regulates PI3K basal activity, stabilizes the C subunit, and plays a role in the activation downstream of tyrosine kinases. All R subunits contain two SH2 domains that flank an intervening helical domain (iSH2), which binds to the N-terminal adaptor-binding domain (ABD) of the catalytic subunit. p85beta, also called PIK3R2, contains N-terminal SH3 and GAP domains. It is expressed ubiquitously but at lower levels than p85alpha. Its expression is increased in breast and colon cancer, correlates with tumor progression, and enhanced invasion. During viral infection, the viral nonstructural (NS1) protein binds p85beta specifically, which leads to PI3K activation and the promotion of viral replication. Mice deficient with PIK3R2 develop normally and exhibit moderate metabolic and immunological defects.
Pssm-ID: 214019 [Multi-domain] Cd Length: 161 Bit Score: 40.07 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 122 LGQQLQLKVQRLHDIETENQKLretLEEYNKEFAEVKNQEVTIKALKEKIREYEQtlknQAETialekEQKLQNDFAEKE 201
Cdd:cd12926 6 VGAQLKVYHQQYQDKSREYDQL---YEEYTRTSQELQMKRTAIEAFNETIKIFEE----QGQT-----QEKCSKEYLERF 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622917383 202 RKlqetqmsttsklEEAEHKVQSLQTALEKTR---TELFDLKTKYDEETTAKAD---EIEMIMTDLE 262
Cdd:cd12926 74 RR------------EGNEKEMQRILLNSERLKsriAEIHESRTKLEQDLRAQASdnrEIDKRMNSLK 128
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
126-236 |
2.93e-03 |
|
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).
Pssm-ID: 464620 [Multi-domain] Cd Length: 276 Bit Score: 41.23 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 126 LQLKVQRLHDietENQKLRETLEEYNKEFAEVKNQEVTI-KALKEKIREYEQT---LKNQAETIALE-KEQKLQNDFAEK 200
Cdd:pfam15294 131 LHMEIERLKE---ENEKLKERLKTLESQATQALDEKSKLeKALKDLQKEQGAKkdvKSNLKEISDLEeKMAALKSDLEKT 207
|
90 100 110
....*....|....*....|....*....|....*.
gi 1622917383 201 ERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTEL 236
Cdd:pfam15294 208 LNASTALQKSLEEDLASTKHELLKVQEQLEMAEKEL 243
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
51-370 |
2.99e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 42.13 E-value: 2.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 51 ESEQSRKRLIEQSREfkknTPEDLRKQVapLLKSFQ-GE-IDALSKRSKEAEAAFlNVYKRLIDVPDPV----------- 117
Cdd:PRK04778 133 ESEEKNREEVEQLKD----LYRELRKSL--LANRFSfGPaLDELEKQLENLEEEF-SQFVELTESGDYVeareildqlee 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 118 ------------PAL------DLGQQL--------QLKVQ-----------RLHDIETENQKLRETLEEYNKEFAEVKNQ 160
Cdd:PRK04778 206 elaaleqimeeiPELlkelqtELPDQLqelkagyrELVEEgyhldhldiekEIQDLKEQIDENLALLEELDLDEAEEKNE 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 161 EvtikaLKEKIRE-YEQtlknqaetiaLEKEQKLQNdfaekerklqetqmsttskleEAEHKVQSLQTALEKTRTELFDL 239
Cdd:PRK04778 286 E-----IQERIDQlYDI----------LEREVKARK---------------------YVEKNSDTLPDFLEHAKEQNKEL 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 240 KTKydeettakadeiemimtdLERANQRAEVAQREAETLR---EQLSSANHSLQlasQIQKAPDvEQAIevlTRSSLEVE 316
Cdd:PRK04778 330 KEE------------------IDRVKQSYTLNESELESVRqleKQLESLEKQYD---EITERIA-EQEI---AYSELQEE 384
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622917383 317 LAAKEREIAQLVEDVQRLQASLTKLR--ENSASQ-ISQLEQQLsaknSTLKQLEEKL 370
Cdd:PRK04778 385 LEEILKQLEEIEKEQEKLSEMLQGLRkdELEAREkLERYRNKL----HEIKRYLEKS 437
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
43-358 |
3.09e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 42.35 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 43 TVLANRQDESEQSRKRLiEQSREFKknTPEDlrkqvAPLLKSFQGEIDALSKRSKEAEAAflNVYKRLIDvpdpvpaldl 122
Cdd:PRK10929 16 GAYAATAPDEKQITQEL-EQAKAAK--TPAQ-----AEIVEALQSALNWLEERKGSLERA--KQYQQVID---------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 123 gqqlqlkvqrlhDIETENQKLRETLEEYNKEFAEVkNQEVTIKALKEKIREYEQTLKNQAETiaLEKEQKLQNDFAEKER 202
Cdd:PRK10929 76 ------------NFPKLSAELRQQLNNERDEPRSV-PPNMSTDALEQEILQVSSQLLEKSRQ--AQQEQDRAREISDSLS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 203 KLQETQMSTTSKLEEAEHKVQSL--------QTALEKTRTELFDLKtkydeettAKADEIEMIMTDL----ERANQRAEV 270
Cdd:PRK10929 141 QLPQQQTEARRQLNEIERRLQTLgtpntplaQAQLTALQAESAALK--------ALVDELELAQLSAnnrqELARLRSEL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 271 AQREAETLREQLSSANHslQLASQIQKapDVEQAIEvltrsslEVELAAKE---------------REIAQ-LVEDVQRL 334
Cdd:PRK10929 213 AKKRSQQLDAYLQALRN--QLNSQRQR--EAERALE-------STELLAEQsgdlpksivaqfkinRELSQaLNQQAQRM 281
|
330 340
....*....|....*....|....
gi 1622917383 335 QASLTKLREnSASQISQLEQQLSA 358
Cdd:PRK10929 282 DLIASQQRQ-AASQTLQVRQALNT 304
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
266-425 |
3.20e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 42.25 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 266 QRAEVAQREAETLREQLSSANHSLQ------------LASQIQKA--PDVEQAIEVLTRSSLEVElaakeREIAQLVEDV 331
Cdd:COG3096 785 KRLEELRAERDELAEQYAKASFDVQklqrlhqafsqfVGGHLAVAfaPDPEAELAALRQRRSELE-----RELAQHRAQE 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 332 QRLQASLTKLRENS------------------ASQISQLEQQLSAKNS----------TLKQLEEKLKG----------- 372
Cdd:COG3096 860 QQLRQQLDQLKEQLqllnkllpqanlladetlADRLEELREELDAAQEaqafiqqhgkALAQLEPLVAVlqsdpeqfeql 939
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622917383 373 QADYEEVKKELNILKSMEFAPSEGA------GTQDAAKplevlLMEKNRSLqseNAALR 425
Cdd:COG3096 940 QADYLQAKEQQRRLKQQIFALSEVVqrrphfSYEDAVG-----LLGENSDL---NEKLR 990
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
121-448 |
3.29e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 42.34 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 121 DLGQQLQ-LKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALkEKIREYEQTLKNQAETIALEKEQKLQNDFAE 199
Cdd:PTZ00108 1035 DLVKELKkLGYVRFKDIIKKKSEKITAEEEEGAEEDDEADDEDDEEEL-GAAVSYDYLLSMPIWSLTKEKVEKLNAELEK 1113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 200 KERKLQETQmSTTSK---LEEaehkVQSLQTALEKTRtelfdlktKYDEETTAKADEIEMIMTDLERANQR-----AEVA 271
Cdd:PTZ00108 1114 KEKELEKLK-NTTPKdmwLED----LDKFEEALEEQE--------EVEEKEIAKEQRLKSKTKGKASKLRKpklkkKEKK 1180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 272 QREAETLREQLSSANHSLQLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQ 351
Cdd:PTZ00108 1181 KKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEF 1260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 352 LEQQLSAKNSTLKQLEEKLKGQADYEEVKKELNILKSmeFAPSEGAGTQDA-AKPLEVLLMEKNRSLQSENAALRISNSD 430
Cdd:PTZ00108 1261 SSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESN--GGSKPSSPTKKKvKKRLEGSLAALKKKKKSEKKTARKKKSK 1338
|
330
....*....|....*...
gi 1622917383 431 lSGSARRKGKDQPESRRP 448
Cdd:PTZ00108 1339 -TRVKQASASQSSRLLRR 1355
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
225-387 |
3.40e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 225 LQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSL-QLASQIQKAPDVEQ 303
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELeELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 304 AIEVL-TRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSAsQISQLEQQLSAK-----NSTLKQLEEKLKgqaDYE 377
Cdd:COG4717 127 LLPLYqELEALEAELAELPERLEELEERLEELRELEEELEELEA-ELAELQEELEELleqlsLATEEELQDLAE---ELE 202
|
170
....*....|
gi 1622917383 378 EVKKELNILK 387
Cdd:COG4717 203 ELQQRLAELE 212
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
81-383 |
3.53e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.25 E-value: 3.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 81 LLKSFQGEIDALSKRSKEAEA-------------AFLNVYKRLIDVPDPVPAL-DLGQQLQLKVQRLHDIETENQKLRET 146
Cdd:PRK04863 787 RIEQLRAEREELAERYATLSFdvqklqrlhqafsRFIGSHLAVAFEADPEAELrQLNRRRVELERALADHESQEQQQRSQ 866
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 147 L----------------------EEYNKEFAEVKNQEVTIKALKEKIREYEQTLkNQAETIAlekeQKLQNDfaekerkl 204
Cdd:PRK04863 867 LeqakeglsalnrllprlnlladETLADRVEEIREQLDEAEEAKRFVQQHGNAL-AQLEPIV----SVLQSD-------- 933
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 205 qetqmstTSKLEEAEHKVQSLQTALEKTRTELFDLKT--------KYDEETTAKADEIEMImtdlERANQRAEVAQREAE 276
Cdd:PRK04863 934 -------PEQFEQLKQDYQQAQQTQRDAKQQAFALTEvvqrrahfSYEDAAEMLAKNSDLN----EKLRQRLEQAEQERT 1002
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 277 TLREQLSSANHSLQLASQIQkapdveqaievltrSSLEVELAAKEREIAQLVEDVQRL----------QASLTK------ 340
Cdd:PRK04863 1003 RAREQLRQAQAQLAQYNQVL--------------ASLKSSYDAKRQMLQELKQELQDLgvpadsgaeeRARARRdelhar 1068
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1622917383 341 LRENSaSQISQLEQQLSAKNSTLKQLEEKL-KGQADYEEVKKEL 383
Cdd:PRK04863 1069 LSANR-SRRNQLEKQLTFCEAEMDNLTKKLrKLERDYHEMREQV 1111
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
249-375 |
3.92e-03 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 41.37 E-value: 3.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 249 AKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASQIQkapdveqaievlTRSSLEVELAAKEREIAQLv 328
Cdd:COG3524 174 AREDAVRFAEEEVERAEERLRDAREALLAFRNRNGILDPEATAEALLQ------------LIATLEGQLAELEAELAAL- 240
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1622917383 329 edvqrlqasLTKLRENSAsQISQLEQQLSAKNSTLKQLEEKLKGQAD 375
Cdd:COG3524 241 ---------RSYLSPNSP-QVRQLRRRIAALEKQIAAERARLTGASG 277
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
313-384 |
4.05e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 4.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 313 LEVELAAKEREIAQLVEDVQRLQASLTKLRENS-------------------ASQISQLEQQ---LSAKNSTLKQLEEKL 370
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQERRealqrlaeyswdeidvasaEREIAELEAElerLDASSDDLAALEEQL 694
|
90
....*....|....*
gi 1622917383 371 KG-QADYEEVKKELN 384
Cdd:COG4913 695 EElEAELEELEEELD 709
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
141-284 |
4.52e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 41.02 E-value: 4.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 141 QKLRETLEEYNKE-FAEVKNQEVTIKALKEKIREYEQTLknQAETIALEKE-----QKLQNDFAEKERK-LQETQMSTTS 213
Cdd:cd16269 149 EDREKLVEKYRQVpRKGVKAEEVLQEFLQSKEAEAEAIL--QADQALTEKEkeieaERAKAEAAEQERKlLEEQQRELEQ 226
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622917383 214 KLEEAEHkvqSLQTALEKtrtelfdLKTKYDEETTAKADEIEMIMTDLERANQR--AEVAQREAETLREQLSS 284
Cdd:cd16269 227 KLEDQER---SYEEHLRQ-------LKEKMEEERENLLKEQERALESKLKEQEAllEEGFKEQAELLQEEIRS 289
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
1339-1421 |
4.59e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 41.70 E-value: 4.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 1339 GQAGASDSPSARSGRAAPSSEGD-----SCDGVEATEGPGSADTEEPKSQGEAEREEAPRPaeqtepPPSGTPGPDDARD 1413
Cdd:PHA03307 283 GPASSSSSPRERSPSPSPSSPGSgpapsSPRASSSSSSSRESSSSSTSSSSESSRGAAVSP------GPSPSRSPSPSRP 356
|
....*...
gi 1622917383 1414 DDHEGGPA 1421
Cdd:PHA03307 357 PPPADPSS 364
|
|
| COG0610 |
COG0610 |
Type I site-specific restriction-modification system, R (restriction) subunit and related ... |
2-258 |
5.38e-03 |
|
Type I site-specific restriction-modification system, R (restriction) subunit and related helicases ... [Defense mechanisms];
Pssm-ID: 440375 [Multi-domain] Cd Length: 936 Bit Score: 41.39 E-value: 5.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 2 SAGAGKGAPQTPVEspTASSKLPQAH----WLCSPGIKRELDATATVL------ANRQDESEQSRKRLIEQSREFKKntp 71
Cdd:COG0610 664 SEEDGKEDVLTDPE--EALEELKEALdelrALFPEGVDFSAFDPTEKLealdeaVERFLGDEEARKEFKKLFKELSR--- 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 72 edLRKQVAPLLKSFQGEIDALSKRSkeaeAAFLNVYKRLIDVPDPVPAldlgQQLQLKVQRLHD--IETENQKLRETLEE 149
Cdd:COG0610 739 --LYNLLSPDDEFGDLELEKYRDDV----SFYLALRAKLRKLGEKLDL----KEYEEKIRQLLDeaIDLERKEIKPRIKQ 808
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 150 ---YNKEFAE--------VKNQEVTIKALKEKIREYEQTLKNQAETIA---LEKEQK-----LQNDFAEKERKLQETQMS 210
Cdd:COG0610 809 npvQYRKFSElleeiieeYNNGALDADEVLEELEELAKEVKEEEERAEeegLNEEELafydaLAENLGDEKLKELAKELD 888
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1622917383 211 TTSKlEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKAdeIEMIM 258
Cdd:COG0610 889 DLLK-KNVTVDWRKRESVRAKLRDAIKRLLRKYGYPKQDEA--VEEVY 933
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
291-387 |
5.49e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.38 E-value: 5.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 291 LASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQAsltklrensasQISQLEQQLSAKNSTLKQLEEKL 370
Cdd:COG2433 382 LEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEA-----------EVEELEAELEEKDERIERLEREL 450
|
90 100
....*....|....*....|.
gi 1622917383 371 K--GQADYEEVKK--ELNILK 387
Cdd:COG2433 451 SeaRSEERREIRKdrEISRLD 471
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
155-324 |
5.79e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 5.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 155 AEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQNDFaEKERKLQEtqmsttSKLEEAEHKVQSLQTALEKtRT 234
Cdd:PRK12704 31 AKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEF-EKELRERR------NELQKLEKRLLQKEENLDR-KL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 235 ELFDLKtkyDEETTAKADEIEMIMTDLEraNQRAEVAQREAETLREqlssanhsLQLASQIQKapdvEQAIEVL---TRS 311
Cdd:PRK12704 103 ELLEKR---EEELEKKEKELEQKQQELE--KKEEELEELIEEQLQE--------LERISGLTA----EEAKEILlekVEE 165
|
170
....*....|...
gi 1622917383 312 SLEVELAAKEREI 324
Cdd:PRK12704 166 EARHEAAVLIKEI 178
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
42-381 |
6.12e-03 |
|
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: 41.19 E-value: 6.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 42 ATVLANRQDESEQSRKRLIEQSREFK--KNTPEDLRKQ---VAPLLKSFQ------GEIDALSKRSKEAEAAFLNVYKRL 110
Cdd:TIGR00606 736 QSIIDLKEKEIPELRNKLQKVNRDIQrlKNDIEEQETLlgtIMPEEESAKvcltdvTIMERFQMELKDVERKIAQQAAKL 815
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 111 IDVPDPVPALDLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREyeqtlknqaetiALEKE 190
Cdd:TIGR00606 816 QGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGT------------NLQRR 883
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 191 QKLQNDFAEKERKLQETqmstTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMI----------MTD 260
Cdd:TIGR00606 884 QQFEEQLVELSTEVQSL----IREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIkekvknihgyMKD 959
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 261 LERANQRA---EVAQREAE--TLREQLSSA-------NHSLQLASQIQKAPDVEQAI--EVLTRSSLEVELAAKEREIAQ 326
Cdd:TIGR00606 960 IENKIQDGkddYLKQKETElnTVNAQLEECekhqekiNEDMRLMRQDIDTQKIQERWlqDNLTLRKRENELKEVEEELKQ 1039
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622917383 327 LvedvqrlqasLTKLRENSASQISQLEQQLSAKNSTLKQLEEKLKG-QADYEEVKK 381
Cdd:TIGR00606 1040 H----------LKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGrQKGYEKEIK 1085
|
|
| CCDC144C |
pfam14915 |
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ... |
140-425 |
6.67e-03 |
|
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ankyrin repeat domain-containing protein 26-like 1 found in eukaryotes. Its function remains unknown, however, it is known to contain a coiled-coil domain which corresponds to this region. The ankyrin repeat which features in this protein is a common amino acid motif.
Pssm-ID: 464371 [Multi-domain] Cd Length: 304 Bit Score: 40.36 E-value: 6.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 140 NQKLRETLEEYNKEFAEVKNQEVT--------IKALKEKIREYEQTLKNQAETIA---LEKEQKLQNDFAEKERklqetq 208
Cdd:pfam14915 1 NCMLQDEIAMLRLEIDTIKNQNQEkekkyledIEILKEKNDDLQKTLKLNEETLTktvFQYNGQLNVLKAENTM------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 209 msTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKadeiemimTDLERANQRaevAQREAETLREQLSSANHS 288
Cdd:pfam14915 75 --LNSKLENEKQNKERLETEVESYRSRLAAAIQDHEQSQTSK--------RDLELAFQR---ERDEWLRLQDKMNFDVSN 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 289 LQLASQI--QKAPDVEQAIevltrSSLEVEL---AAKEREIAQLVEDVQRlqasltklrensasqisqleqQLSAKNSTL 363
Cdd:pfam14915 142 LRDENEIlsQQLSKAESKA-----NSLENELhrtRDALREKTLLLESVQR---------------------DLSQAQCQK 195
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622917383 364 KQLEEKLkgQADYEEVKKELNILKSMEfapsegagtqdaakplevllmEKNRSLQSENAALR 425
Cdd:pfam14915 196 KELEHMY--QNEQDKVNKYIGKQESLE---------------------ERLAQLQSENMLLR 234
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
124-438 |
6.79e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 41.26 E-value: 6.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 124 QQLQLKVQRLHDIETENQKLRETLEeyNKEFAEVKNQEVTiKALKEKIREYEQTLKNQAETIALEKEQKLQN------DF 197
Cdd:pfam15921 120 QEMQMERDAMADIRRRESQSQEDLR--NQLQNTVHELEAA-KCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEirsilvDF 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 198 AEKERK--LQETQMSTT--SKLEEAEHKV-QSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTD-LERANQRAEVA 271
Cdd:pfam15921 197 EEASGKkiYEHDSMSTMhfRSLGSAISKIlRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQhQDRIEQLISEH 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 272 QREAETLREQLSSANhslqlasqiQKAPDVEQAIEVLTRSSLEvELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQ 351
Cdd:pfam15921 277 EVEITGLTEKASSAR---------SQANSIQSQLEIIQEQARN-QNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEE 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 352 LEQQLSAKNSTLKQ--------------LEEKL-KGQADYEEVKKELNILKSM-EFAPSEGAGTQDAAKPLEVLLMEKNR 415
Cdd:pfam15921 347 LEKQLVLANSELTEarterdqfsqesgnLDDQLqKLLADLHKREKELSLEKEQnKRLWDRDTGNSITIDHLRRELDDRNM 426
|
330 340
....*....|....*....|...
gi 1622917383 416 SLQSENAALRISNSDLSGSARRK 438
Cdd:pfam15921 427 EVQRLEALLKAMKSECQGQMERQ 449
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
129-447 |
6.84e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 40.88 E-value: 6.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 129 KVQRLHDIETENQKLRETLEEYNKEFaevKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQNDFAEKERKLQETQ 208
Cdd:pfam17380 235 KMERRKESFNLAEDVTTMTPEYTVRY---NGQTMTENEFLNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKARE 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 209 MSTTSKLEEAEHKVQSL------------QTALEKTRT-ELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREA 275
Cdd:pfam17380 312 VERRRKLEEAEKARQAEmdrqaaiyaeqeRMAMERERElERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKN 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 276 ETLREQLSSANHSLQLASQIQKAPDVEQAIEVLTRSSLEvelAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQ 355
Cdd:pfam17380 392 ERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQE---EARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQ 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 356 LSAKNSTLKQLEEKLKGQADYEEVKKELnILKSMEFAPSEGAGTQDAAKPLEVLLMEKNRSLQSENAAlRISNSDlsgsa 435
Cdd:pfam17380 469 EEERKRKKLELEKEKRDRKRAEEQRRKI-LEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERR-REAEEE----- 541
|
330
....*....|..
gi 1622917383 436 RRKGKDQPESRR 447
Cdd:pfam17380 542 RRKQQEMEERRR 553
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
139-395 |
7.20e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 41.26 E-value: 7.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 139 ENQK--LRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQaetialekeqkLQNDFAEKE--RKLQETQMS-TTS 213
Cdd:pfam15921 102 EKQKfyLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQ-----------LQNTVHELEaaKCLKEDMLEdSNT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 214 KLEEAEHKVQSLQTALEKTRTELFDL-----KTKYDEET----------TAKADEIEMIMTDLERANQRAEVAQREAETL 278
Cdd:pfam15921 171 QIEQLRKMMLSHEGVLQEIRSILVDFeeasgKKIYEHDSmstmhfrslgSAISKILRELDTEISYLKGRIFPVEDQLEAL 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 279 ReqlSSANHSLQLASQiQKAPDVEQAIevltrSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLSA 358
Cdd:pfam15921 251 K---SESQNKIELLLQ-QHQDRIEQLI-----SEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSD 321
|
250 260 270
....*....|....*....|....*....|....*...
gi 1622917383 359 KNSTLKQLEEKLK-GQADYEEVKKELNilKSMEFAPSE 395
Cdd:pfam15921 322 LESTVSQLRSELReAKRMYEDKIEELE--KQLVLANSE 357
|
|
| Wtap |
pfam17098 |
WTAP/Mum2p family; The Wtap family includes female-lethal(2)D from Drosophila and ... |
311-429 |
7.87e-03 |
|
WTAP/Mum2p family; The Wtap family includes female-lethal(2)D from Drosophila and pre-mRNA-splicing regulator WTAP from mammals. The former is required for female-specific splicing of Sex-lethal RNA, and the latter is a regulatory subunit of the RNA N6-methyladenosine methyltransferase. The family also includes the yeast Mum2p protein which is part of the Mis complex.
Pssm-ID: 465345 [Multi-domain] Cd Length: 155 Bit Score: 38.82 E-value: 7.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 311 SSLEVELAAKEREIAQLVEDVQRLQASLTKlrENSASQISQLEQQLSAKNSTLKQLEEKLKgqADYEEVKKELNILKsme 390
Cdd:pfam17098 7 NLLLARLAEKEQEIQELKAQLQDLKQSLQP--PSSQLRSLLLDPAVNLEFLRLKKELEEKK--KKLKEAQLELAAWK--- 79
|
90 100 110
....*....|....*....|....*....|....*....
gi 1622917383 391 FAPSEGAGTQdaakplevlLMEKNRSLQSENAALRISNS 429
Cdd:pfam17098 80 FTPDSTTGKR---------LMAKCRLLQQENEELGRQLS 109
|
|
| DUF4201 |
pfam13870 |
Domain of unknown function (DUF4201); This is a family of coiled-coil proteins from eukaryotes. ... |
136-267 |
8.20e-03 |
|
Domain of unknown function (DUF4201); This is a family of coiled-coil proteins from eukaryotes. The function is not known.
Pssm-ID: 464008 [Multi-domain] Cd Length: 177 Bit Score: 39.13 E-value: 8.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 136 IETENQKLRETLEEYNKEFAEVKNQEV----TIKALKEKIREYEQTLKNQAETIAlekeqKLQNDFAEKERKLQETQMsT 211
Cdd:pfam13870 47 LQIENQALNEKIEERNKELKRLKLKVTntvhALTHLKEKLHFLSAELSRLKKELR-----ERQELLAKLRKELYRVKL-E 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622917383 212 TSKLEEAEHKVqslqtaleKTRTELF---DLKTKYD---EETTAKADEIEMIMTDLERANQR 267
Cdd:pfam13870 121 RDKLRKQNKKL--------RQQGGLLhvpALLHDYDktkAEVEEKRKSVKKLRRKVKILEMR 174
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
136-369 |
8.34e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.93 E-value: 8.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 136 IETENQKLRETLEEYNKEFAEVKNQ----EVTIKALKEKIREyEQTLKNQAetiaLEKEQKLQNDFAEkerkLQETQMST 211
Cdd:pfam01576 213 LEGESTDLQEQIAELQAQIAELRAQlakkEEELQAALARLEE-ETAQKNNA----LKKIRELEAQISE----LQEDLESE 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 212 TSKLEEAEHKVQSLQTALEKTRTELFD----------LKTKYDEETT--AKADEIEMIMTDleraNQRAEVAQREA---E 276
Cdd:pfam01576 284 RAARNKAEKQRRDLGEELEALKTELEDtldttaaqqeLRSKREQEVTelKKALEEETRSHE----AQLQEMRQKHTqalE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 277 TLREQLSSANH---SLQLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLE 353
Cdd:pfam01576 360 ELTEQLEQAKRnkaNLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQ 439
|
250
....*....|....*.
gi 1622917383 354 QQLSAKNSTLKQLEEK 369
Cdd:pfam01576 440 SELESVSSLLNEAEGK 455
|
|
| Homeobox_KN |
pfam05920 |
Homeobox KN domain; This is a homeobox transcription factor KN domain conserved from fungi to ... |
1289-1323 |
8.43e-03 |
|
Homeobox KN domain; This is a homeobox transcription factor KN domain conserved from fungi to human and plants. They were first identified as TALE homeobox genes in eukaryotes, (including KNOX and MEIS genes). They have been recently classified.
Pssm-ID: 428673 Cd Length: 39 Bit Score: 35.57 E-value: 8.43e-03
10 20 30
....*....|....*....|....*....|....*
gi 1622917383 1289 QQKPYPSPKTIEDLATQLNLKTSTVINWFHNYRSR 1323
Cdd:pfam05920 5 LHNPYPSEEEKAELAKETGLSRKQISNWFINARRR 39
|
|
| Nuf2_DHR10-like |
pfam18595 |
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ... |
124-226 |
8.44e-03 |
|
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This domain was identified as MazG related domain also designated as Designed helical repeat protein 10 (DHR10) that actually adopts a coiled-coil structure. Nuf2 is part of the Ndc80 complex, which binds to the spindle and is required for chromosome segregation and spindle checkpoint activity.
Pssm-ID: 465814 [Multi-domain] Cd Length: 117 Bit Score: 37.95 E-value: 8.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 124 QQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREyeqtlkNQAETIALE-KEQKLQNDFAEKER 202
Cdd:pfam18595 19 RELQAKIDALQVVEKDLRSCIKLLEEIEAELAKLEEAKKKLKELRDALEE------KEIELRELErREERLQRQLENAQE 92
|
90 100
....*....|....*....|....
gi 1622917383 203 KLQETQMSTTSKLEEAEHKVQSLQ 226
Cdd:pfam18595 93 KLERLREQAEEKREAAQARLEELR 116
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
121-292 |
9.03e-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: 40.71 E-value: 9.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 121 DLGQQLQlkvQRLHDIETENQKLRETLE-------EYNKEFA------EVKNQevTIKALKEKIREYEQTLKNQAETIAL 187
Cdd:COG3096 984 DLNEKLR---ARLEQAEEARREAREQLRqaqaqysQYNQVLAslkssrDAKQQ--TLQELEQELEELGVQADAEAEERAR 1058
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917383 188 EKEQKLQNDF-AEKERKlqeTQMSTTSKLEEAEhkVQSLQTALEKTRTELFDLKTkydEETTAKA---DEIEMIM-TDLE 262
Cdd:COG3096 1059 IRRDELHEELsQNRSRR---SQLEKQLTRCEAE--MDSLQKRLRKAERDYKQERE---QVVQAKAgwcAVLRLARdNDVE 1130
|
170 180 190
....*....|....*....|....*....|
gi 1622917383 263 RANQRAEVAQREAETLREQLSSANHSLQLA 292
Cdd:COG3096 1131 RRLHRRELAYLSADELRSMSDKALGALRLA 1160
|
|
|