|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
37-417 |
1.00e-13 |
|
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: 1.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 37 LTRQVHKLEYSAEQEER---LKKELEAA-----TDRIKQLEENFEAeraahlkskFNLEITQMRIRELEGALQMekvsqA 108
Cdd:TIGR02168 198 LERQLKSLERQAEKAERykeLKAELRELelallVLRLEELREELEE---------LQEELKEAEEELEELTAEL-----Q 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 109 EALSDLEMIRKEFKEVENAYEREKQKAQENLEKVNRLEREYISTNKQMNEKIEEKKEiikdLSERLQENEKIHRELQDKL 188
Cdd:TIGR02168 264 ELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE----LEAQLEELESKLDELAEEL 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 189 ATAKKhqvfVTETYENNMIELKLLLDSFAmsgqrtagtckdKDKPSSLSVLETLRYTLTAYQNKLEDTSNELKKMNALCE 268
Cdd:TIGR02168 340 AELEE----KLEELKEELESLEAELEELE------------AELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 269 NTTKELEISRDKMCVLSQDLKEARDKLANANKELnhLHTECADKAALIGTLQMELQNVQQRWEEEKVRAAESENEIQKLT 348
Cdd:TIGR02168 404 RLEARLERLEDRRERLQQEIEELLKKLEEAELKE--LQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAE 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 349 R----------AYKKDMEEKLTFLHGLYQHLVAGcvliKQPEGILDRFS--------WS-ELCAVLQENVDALIL-DLNR 408
Cdd:TIGR02168 482 RelaqlqarldSLERLQENLEGFSEGVKALLKNQ----SGLSGILGVLSelisvdegYEaAIEAALGGRLQAVVVeNLNA 557
|
....*....
gi 2024433733 409 ANEKISHLE 417
Cdd:TIGR02168 558 AKKAIAFLK 566
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
246-952 |
4.56e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 71.24 E-value: 4.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 246 LTAYQNKLEDTSNELKKMNALCENTTKELEisrdkmcVLSQDLKEARDKLANANKELNHLHTECADKAALIGTLQMELQN 325
Cdd:TIGR02168 234 LEELREELEELQEELKEAEEELEELTAELQ-------ELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQI 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 326 VQQRWEEEKVRAAESENEIQKLTRAyKKDMEEKLTflhglyqhlvagcvlikqpegildrfSWSELCAVLQENVDALILD 405
Cdd:TIGR02168 307 LRERLANLERQLEELEAQLEELESK-LDELAEELA--------------------------ELEEKLEELKEELESLEAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 406 LNRANEKISHLEyickSKSDTMKELQRSQEDDMSKMAEQMKAQescwQKQKKYLEQQYSDLlgevharaqeyKETAEKNK 485
Cdd:TIGR02168 360 LEELEAELEELE----SRLEELEEQLETLRSKVAQLELQIASL----NNEIERLEARLERL-----------EDRRERLQ 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 486 EKICVLEKRQEELALENlyVKNTLTQIQKEHSSLLAACALLAGALYPLYGRSCAMSIQRDLLQDQVNIYelvNQEIRTLV 565
Cdd:TIGR02168 421 QEIEELLKKLEEAELKE--LQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQL---QARLDSLE 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 566 HILSGVEEEKEDDAKIKKHKFRG---------LIHV---FRRGVIAVLAANRLKVLAQSSSSLFSLINGFKE--GIGILV 631
Cdd:TIGR02168 496 RLQENLEGFSEGVKALLKNQSGLsgilgvlseLISVdegYEAAIEAALGGRLQAVVVENLNAAKKAIAFLKQneLGRVTF 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 632 CVGDSKgKHNMSRYNKEgircvEALNWFTSP-DLLTAVISSVTELQDVISKtdpkscLSGRLLVS---AARNSFSKLMDK 707
Cdd:TIGR02168 576 LPLDSI-KGTEIQGNDR-----EILKNIEGFlGVAKDLVKFDPKLRKALSY------LLGGVLVVddlDNALELAKKLRP 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 708 LNVImesVPLDSsrsvtyveknsliqrlahglHRINARALEAGScDRRPIMkSIASLQKQIAEFTQRLHTVEVERCSLRR 787
Cdd:TIGR02168 644 GYRI---VTLDG--------------------DLVRPGGVITGG-SAKTNS-SILERRREIEELEEKIEELEEKIAELEK 698
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 788 ELAEFKLNFSKMKQEADKAQSLKE----QLSLFKQSKLIAHKRFESACEELNNALHWEHQAQVLLNEQAQQLQELNNKLE 863
Cdd:TIGR02168 699 ALAELRKELEELEEELEQLRKELEelsrQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELA 778
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 864 LHSSE----EADKNQVLSETV---KRLSEAKMELRRKDQSLRQLNRLLTQLEQDKRRLKESIHDAESALCMAAKDRELII 936
Cdd:TIGR02168 779 EAEAEieelEAQIEQLKEELKalrEALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLA 858
|
730
....*....|....*.
gi 2024433733 937 NQMKSVEATLHTVRDQ 952
Cdd:TIGR02168 859 AEIEELEELIEELESE 874
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
43-348 |
2.86e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 68.54 E-value: 2.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 43 KLEYSAEQEERLKKELEAATDRIKQLEENFEAERAAHLKSKFNLEITQMRIRELEGALQmekvSQAEALSDLEMIRKEFK 122
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE----QLEERIAQLSKELTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 123 EVENAYEREKQKAQENLEkvnRLEREYISTNKQMNekieekkeiikDLSERLQENEKIHRELQDKLATAKKHQVFVTETY 202
Cdd:TIGR02168 761 AEIEELEERLEEAEEELA---EAEAEIEELEAQIE-----------QLKEELKALREALDELRAELTLLNEEAANLRERL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 203 ENNMIELKLLLDSFAMSGQRTAGTckdKDKPSSLSV-LETLRYTLTAYQNKLEDTSNELKKMNALCENTTKELEISRDKM 281
Cdd:TIGR02168 827 ESLERRIAATERRLEDLEEQIEEL---SEDIESLAAeIEELEELIEELESELEALLNERASLEEALALLRSELEELSEEL 903
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024433733 282 CVLSQDLKEARDKLANANKELNHLHTECAdkaaligTLQMELQNVQQR-WEEEKVRAAESENEIQKLT 348
Cdd:TIGR02168 904 RELESKRSELRRELEELREKLAQLELRLE-------GLEVRIDNLQERlSEEYSLTLEEAEALENKIE 964
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
48-507 |
3.51e-08 |
|
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: 58.21 E-value: 3.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 48 AEQEERLKKELEAATDRIKQLEENFE------AERAAHLKSKFN-----LEITQMRIRElEGALQMEKVSQAEalSDLEM 116
Cdd:pfam15921 252 SESQNKIELLLQQHQDRIEQLISEHEveitglTEKASSARSQANsiqsqLEIIQEQARN-QNSMYMRQLSDLE--STVSQ 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 117 IRKEFKEVENAYErekqkaqenlEKVNRLEREYISTNKQMNEKIEEKKEIIkdlserlQENEKIHRELQDKLATAKKHQV 196
Cdd:pfam15921 329 LRSELREAKRMYE----------DKIEELEKQLVLANSELTEARTERDQFS-------QESGNLDDQLQKLLADLHKREK 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 197 FVTETYENNmielKLLLDsfamsgqrtagtckdKDKPSSLsvletlryTLTAYQNKLEDTSNELKKMNALCENTTKELEI 276
Cdd:pfam15921 392 ELSLEKEQN----KRLWD---------------RDTGNSI--------TIDHLRRELDDRNMEVQRLEALLKAMKSECQG 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 277 SRDKMCVLSQDLKEARDKLANANKELNHLHTECADKAALIGTLQMELQNVQQRWE------EEKVRAAESEN-EIQKLTR 349
Cdd:pfam15921 445 QMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSdltaslQEKERAIEATNaEITKLRS 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 350 AYKKDMEEkltflhglYQHLvagcvlikQPEGildrfswsELCAVLQENVDALILDLnranekishleyickSKSDTMKE 429
Cdd:pfam15921 525 RVDLKLQE--------LQHL--------KNEG--------DHLRNVQTECEALKLQM---------------AEKDKVIE 565
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024433733 430 LQRSQEDDMSKMAEQMKAQESCWQKQKKYLEQQYSDLLGEVharaQEYKETAEKNKEKICVLEKRQEELALENLYVKN 507
Cdd:pfam15921 566 ILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLEL----QEFKILKDKKDAKIRELEARVSDLELEKVKLVN 639
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
96-350 |
8.14e-07 |
|
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: 52.84 E-value: 8.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 96 LEGALQMEKVSQAEAlsDLEMIRKEFKEVENAYEREKQKAQENLEKVNRLEREYISTNKQMNEKIEEKKeiikDLSERLQ 175
Cdd:COG4942 13 LAAAAQADAAAEAEA--ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELA----ALEAELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 176 ENEKIHRELQDKLATAKKhqvfvtetyennmiELKLLLDSFAMSGQRTAGTC--KDKDKPSSLSVLETLRYTLTAYQNKL 253
Cdd:COG4942 87 ELEKEIAELRAELEAQKE--------------ELAELLRALYRLGRQPPLALllSPEDFLDAVRRLQYLKYLAPARREQA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 254 EDTSNELKKMNALcentTKELEISRDKMCVLSQDLKEARDKLANANKElnhlhtecadKAALIGTLQMELQNVQQRWEEE 333
Cdd:COG4942 153 EELRADLAELAAL----RAELEAERAELEALLAELEEERAALEALKAE----------RQKLLARLEKELAELAAELAEL 218
|
250
....*....|....*..
gi 2024433733 334 KVRAAESENEIQKLTRA 350
Cdd:COG4942 219 QQEAEELEALIARLEAE 235
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
21-359 |
8.35e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.79 E-value: 8.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 21 KKMKDME--LEhRdCSDL---LTRQVHKLEYSAEQEER---LKKELeaatdRIKQLEENFEAERAAHLKskfnLEITQMR 92
Cdd:COG1196 179 RKLEATEenLE-R-LEDIlgeLERQLEPLERQAEKAERyreLKEEL-----KELEAELLLLKLRELEAE----LEELEAE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 93 IRELEGALQMEKVSQAEALSDLEMIRKEFKEVENAYEREKQKAQENLEKVNRLEREYISTNKQMNekieekkeiikDLSE 172
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR-----------ELEE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 173 RLQENEKIHRELQDKLATAKKHQVFVTETYENNMIELKLLLDSFAMSGQRTAGTCKDKDkpSSLSVLETLRYTLTAYQNK 252
Cdd:COG1196 317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA--EAEEELEELAEELLEALRA 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 253 LEDTSNELKKMNALCENTTKELEISRDKMCVLSQDLKEARDKLANANKELNHLHTECADKAALIgtLQMELQNVQQRWEE 332
Cdd:COG1196 395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE--EALLELLAELLEEA 472
|
330 340
....*....|....*....|....*..
gi 2024433733 333 EKVRAAESENEIQKLTRAYKKDMEEKL 359
Cdd:COG1196 473 ALLEAALAELLEELAEAAARLLLLLEA 499
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
10-193 |
1.19e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.40 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 10 KKQNSALQNLSKKMKDMELEHRDCSDLLTRQVHKLEYSAEQEERLKKELEAATDRIKQLEENFEAERAAHLKSKFNLEIT 89
Cdd:COG1196 256 EELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEEL 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 90 QMRIRELEGALqmekvsqAEALSDLEMIRKEFKEVENAYEREKQKAQENLEKVNRLEREYISTNKQMNEKIEEKKEIIKD 169
Cdd:COG1196 336 EEELEELEEEL-------EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408
|
170 180
....*....|....*....|....
gi 2024433733 170 LSERLQENEKIHRELQDKLATAKK 193
Cdd:COG1196 409 EEALLERLERLEEELEELEEALAE 432
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
17-195 |
1.51e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.02 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 17 QNLSKKMKDME-----LEHRDCSDLLTRQVHKLEYSAEQEERLKKELEAATDRIKQLEENFEAERAAHLKSKFNLEITQM 91
Cdd:COG1196 216 RELKEELKELEaelllLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 92 RIRELEGALQMEKVSQAEALSDLEMIRKEFKEVENAYEREKQKAQENLEKVNRLEREYISTNKQMNEKIEEKKEIIKDLS 171
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
170 180
....*....|....*....|....
gi 2024433733 172 ERLQENEKIHRELQDKLATAKKHQ 195
Cdd:COG1196 376 EAEEELEELAEELLEALRAAAELA 399
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
128-952 |
2.31e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 52.38 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 128 YEREKQKAQENLEKVnrleREYISTNKQMnekieekkeiikdLSERLQENEKihreLQDKLATAKKHQVFVTETYEnnmI 207
Cdd:TIGR02169 168 FDRKKEKALEELEEV----EENIERLDLI-------------IDEKRQQLER----LRREREKAERYQALLKEKRE---Y 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 208 ELKLLLDSF-AMSGQRTAGTCKDKDKPSSLSVLETLRYTLTAYQNKLEDTSNEL-KKMNALCENTTKELeisRDKMCVLS 285
Cdd:TIGR02169 224 EGYELLKEKeALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELnKKIKDLGEEEQLRV---KEKIGELE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 286 QDLKEARDKLANANKELNHLHTECADKAALIGTLQMELQNVQQRWEEEKVRAAESENEIQKLTRAYKK---DMEEKLTFL 362
Cdd:TIGR02169 301 AEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDlraELEEVDKEF 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 363 HGLYQHLVAgcvLIKQPEGILDRFSwselcaVLQENVDALILDLNRANEKISHLEYICKSKSDTMKELQRSQEDDMSKMA 442
Cdd:TIGR02169 381 AETRDELKD---YREKLEKLKREIN------ELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIK 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 443 EQMKAQESCWQKQKKYlEQQYSDLlgevharaqeyketaeknKEKICVLEKRQEELALENLYVKNTLTQIQKEHSsllaa 522
Cdd:TIGR02169 452 KQEWKLEQLAADLSKY-EQELYDL------------------KEEYDRVEKELSKLQRELAEAEAQARASEERVR----- 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 523 callagalyplYGRScamsiQRDLLQDQVN-IYELVNQEIR------TLVHILSG-----VEEEKEDDAK--IKKHKFRg 588
Cdd:TIGR02169 508 -----------GGRA-----VEEVLKASIQgVHGTVAQLGSvgeryaTAIEVAAGnrlnnVVVEDDAVAKeaIELLKRR- 570
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 589 lihvfRRGVIAVLAANRLKvlaqSSSSLFSLI--NGFkegIGILVcvgdskgkhNMSRYNKEgircVEALNWFTSPDllT 666
Cdd:TIGR02169 571 -----KAGRATFLPLNKMR----DERRDLSILseDGV---IGFAV---------DLVEFDPK----YEPAFKYVFGD--T 623
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 667 AVISSVTELQDVISK----------TDPKSCLSGRLLVSAARNSFSKlMDKLNVIMESVPLDSSRSvtyvEKNSLIQRLA 736
Cdd:TIGR02169 624 LVVEDIEAARRLMGKyrmvtlegelFEKSGAMTGGSRAPRGGILFSR-SEPAELQRLRERLEGLKR----ELSSLQSELR 698
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 737 HGLHRINA--RALEAGSCDRRPIMKSIASLQKQIAEFTQRLHTVEVERCSLRRELAEFK-----LNFSKMKQEADKAQsL 809
Cdd:TIGR02169 699 RIENRLDElsQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKselkeLEARIEELEEDLHK-L 777
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 810 KEQLSLFKQSKLIA---------------HKRFESACEELNNALHWEHQAQVLLNEQAQQLQELNNKLELHSSEEADKnq 874
Cdd:TIGR02169 778 EEALNDLEARLSHSripeiqaelskleeeVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKE-- 855
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024433733 875 vLSETVKRLSEAKMELRRKDQSLRQLNRLLTQLEQDKRRLKESIHDAESALCMAAKDRELIINQMKSVEATLHTVRDQ 952
Cdd:TIGR02169 856 -IENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEE 932
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
16-498 |
3.32e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.60 E-value: 3.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 16 LQNLSKKMKDMElEHRDCSDLLTRQVHKLEYSAEQ-EERLK-------------KELEAATDRIKQLEENFE------AE 75
Cdd:PRK03918 223 LEKLEKEVKELE-ELKEEIEELEKELESLEGSKRKlEEKIReleerieelkkeiEELEEKVKELKELKEKAEeyiklsEF 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 76 RAAHLKSKFNLEITQMRIRELEGALQmEKVSQAEAL-SDLEMIRKEFKEVENAYEREKQKA---QENLEKVNRLEReyiS 151
Cdd:PRK03918 302 YEEYLDELREIEKRLSRLEEEINGIE-ERIKELEEKeERLEELKKKLKELEKRLEELEERHelyEEAKAKKEELER---L 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 152 TNKQMNEKIEEKKEIIKDLSERLQENEKIHRELQDKLATAKKhqvfVTETYENNMIELKllldsfamSGQRTAGTCKDK- 230
Cdd:PRK03918 378 KKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKK----EIKELKKAIEELK--------KAKGKCPVCGREl 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 231 DKPSSLSVLEtlRYTLtayqnKLEDTSNELKKMNALCE---NTTKELEISRDKMCVLSQdLKEARDKLANANKELNHLHT 307
Cdd:PRK03918 446 TEEHRKELLE--EYTA-----ELKRIEKELKEIEEKERklrKELRELEKVLKKESELIK-LKELAEQLKELEEKLKKYNL 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 308 ECADKAA--------LIGTLQMELQNVQQRWEEEKvraaESENEIQKLTRAyKKDMEEKLTFLHGLYQHLVAGCVL---- 375
Cdd:PRK03918 518 EELEKKAeeyeklkeKLIKLKGEIKSLKKELEKLE----ELKKKLAELEKK-LDELEEELAELLKELEELGFESVEelee 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 376 -IKQPEGILDRF-----SWSELcAVLQENVDALILDLNRANEKISHLEYICKSKSDTMKELQRS-QEDDMSKMAEQMKAQ 448
Cdd:PRK03918 593 rLKELEPFYNEYlelkdAEKEL-EREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKySEEEYEELREEYLEL 671
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2024433733 449 ESCWQKQKKYLEqqysdllgEVHARAQEYKETAEKNKEKICVLEKRQEEL 498
Cdd:PRK03918 672 SRELAGLRAELE--------ELEKRREEIKKTLEKLKEELEEREKAKKEL 713
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
727-990 |
3.35e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.86 E-value: 3.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 727 EKNSLIQRLAHGLHRINARALEAGScDRRPIMKSIASLQKQIAEFTQRLHTVEVERCSLRRELAEFKLNFSKMKQEADKA 806
Cdd:COG1196 264 ELEAELEELRLELEELELELEEAQA-EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEEL 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 807 QSLKEQLSLFKQSKLIAHKRFESACEELNNALH-WEHQAQVLLNEQAQQLQELNNKLELHSSEEADKNQVLSETVKRLSE 885
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAeAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 886 AKMELRRKDQSLRQLNRLLTQLEQDKRRLKESIHDAESALCMAAKDRELIINQMKSVEATLHTVRDQTLLSWTAATRNDF 965
Cdd:COG1196 423 LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
250 260
....*....|....*....|....*
gi 2024433733 966 TLQLPKLHLETFAVEGLKGGPEVVA 990
Cdd:COG1196 503 YEGFLEGVKAALLLAGLRGLAGAVA 527
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
7-196 |
6.17e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.83 E-value: 6.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 7 QSCKKQNSALQNLSKKMKDMELEHRDCSDLLTRQVHKLEYSAEQEERLKKELEAATDRIKQLEENFEA--ERAAHLKSKF 84
Cdd:TIGR02168 253 EELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEEleAQLEELESKL 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 85 NleitqmrirELEGALQMEKVSQAEALSDLEMIRKEFKEVENAYEREKQKAQENLEKVNRLEREYISTNKQMNEKI---E 161
Cdd:TIGR02168 333 D---------ELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNneiE 403
|
170 180 190
....*....|....*....|....*....|....*
gi 2024433733 162 EKKEIIKDLSERLQENEKIHRELQDKLATAKKHQV 196
Cdd:TIGR02168 404 RLEARLERLEDRRERLQQEIEELLKKLEEAELKEL 438
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
10-359 |
8.94e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 8.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 10 KKQNSALQNLSKKMKDMELEhrdcsdlLTRQVHKLEYSAEQEERLKKELEAATDRIKQLEENFEA------ERAAHLKSK 83
Cdd:PRK03918 182 EKFIKRTENIEELIKEKEKE-------LEEVLREINEISSELPELREELEKLEKEVKELEELKEEieelekELESLEGSK 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 84 FNLEItqmRIRELEGALQmEKVSQAEALSDLEMIRKEFKEVENAYEREKQKAQENLEKVNRLEREYISTNKQMNeKIEEK 163
Cdd:PRK03918 255 RKLEE---KIRELEERIE-ELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEIN-GIEER 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 164 KEIIKDLSERLQENEKIHRELQDKLATAKKHQvfvtETYEnnmiELKLLLDSfaMSGQRTAGTCKDKDK-PSSLSVLETL 242
Cdd:PRK03918 330 IKELEEKEERLEELKKKLKELEKRLEELEERH----ELYE----EAKAKKEE--LERLKKRLTGLTPEKlEKELEELEKA 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 243 RYTLTAYQNKLEDTSNELKKMNALCENTTKELEISRDKMCVLSQDLKEARDK--LANANKELNHLHTECADKAALIGTLQ 320
Cdd:PRK03918 400 KEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKelLEEYTAELKRIEKELKEIEEKERKLR 479
|
330 340 350
....*....|....*....|....*....|....*....
gi 2024433733 321 MELQNVqqrweeEKVRAAESENEIQKLTRAYKKDMEEKL 359
Cdd:PRK03918 480 KELREL------EKVLKKESELIKLKELAEQLKELEEKL 512
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
12-303 |
1.15e-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: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 12 QNSALQNLSKKMKDMELEHRDCSDLLTRQVHKLEYSAEQEERLKKELEAATDRIKQLEENFEAERAAHLKSKFNLEITQM 91
Cdd:TIGR02168 724 LSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRE 803
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 92 RIRELEGALQMEKVSQAEALSDLEMIRKEFKEVENAYEREKQKAQENLEKVNRLEREYISTN-----------------K 154
Cdd:TIGR02168 804 ALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEelieeleseleallnerA 883
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 155 QMNEKIEEKKEIIKDLSERLQENEKIHRELQDKLATAKKHQvfvtETYENNMIELKL----LLDSFAMSGQRT---AGTC 227
Cdd:TIGR02168 884 SLEEALALLRSELEELSEELRELESKRSELRRELEELREKL----AQLELRLEGLEVridnLQERLSEEYSLTleeAEAL 959
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024433733 228 KDKDKPSSlsvlETLRYTLTAYQNKLedtsNELKKMNALCENTTKELEISRDKMCVLSQDLKEARDKLANANKELN 303
Cdd:TIGR02168 960 ENKIEDDE----EEARRRLKRLENKI----KELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEID 1027
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
761-952 |
1.39e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.94 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 761 IASLQKQIAEFTQRLHTVEVERCSLRRELAEFKlnfSKMKQEADKAQSLKEQLSLFKQSKLIAHKRFESACEELNNALHW 840
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELE---AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 841 EHQAQVLLNEQAQQLQELNNKLELHSSEEADKNQVLSETVKRLSEAKMELRRKDQSLRQLNRLLTQLEQDKRRLKESIHD 920
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
170 180 190
....*....|....*....|....*....|..
gi 2024433733 921 AESALCMAAKDRELIINQMKSVEATLHTVRDQ 952
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEE 422
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
10-215 |
1.62e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.55 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 10 KKQNSALQNLSKKMKDMELEHRDCSDLLTRQVHKLEYSAEQEERLKKELEAATDRIKQLEENFEAERAAHLKSKFNLEIT 89
Cdd:COG1196 284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 90 QMRIRELEGALQMEKVSQAEALSDLEMIRKEFKEVENAYEREKQKAQENLEKVNRLEREYISTNKQMNEKIEEKKEIIKD 169
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2024433733 170 LSERLQENEKIHRELQdKLATAKKHQVFVTETYENNMIELKLLLDS 215
Cdd:COG1196 444 LEEAAEEEAELEEEEE-ALLELLAELLEEAALLEAALAELLEELAE 488
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
245-483 |
2.00e-05 |
|
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: 48.61 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 245 TLTAYQNKLEDTSNELKKMNALCENTTKELEISRDKMCVLSQDLKEARDKLANANKELNHLHTECADKAALIGTLQMELQ 324
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 325 NVQQRWEEEKVRAAESeneiqkLTRAYKKDMEEKLTFLhglyqhlvagcVLIKQPEGILDRFSW-SELCAVLQENVDALI 403
Cdd:COG4942 94 ELRAELEAQKEELAEL------LRALYRLGRQPPLALL-----------LSPEDFLDAVRRLQYlKYLAPARREQAEELR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 404 LDLNRANEKISHLEYICKSKSDTMKELQRSQEDDMSKMAEQMKAQESCWQKQKKY------LEQQYSDLLGEVHARAQEY 477
Cdd:COG4942 157 ADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELaaelaeLQQEAEELEALIARLEAEA 236
|
....*.
gi 2024433733 478 KETAEK 483
Cdd:COG4942 237 AAAAER 242
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
14-214 |
2.07e-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: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 14 SALQNLSKKMKDMELEHRDCSDLLTRQVHKLEYSAEQEERLKKELEAATDRIKQLEENFEAERAAHLKSKFNLEITQMRI 93
Cdd:COG1196 267 AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 94 RELEGALQMEKVSQAEALSDLEMIRKEFKEVENAYEREKQKAQENLEKVNRLEREYISTNKQMNEKIEEKKEIIKDLSER 173
Cdd:COG1196 347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEEL 426
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2024433733 174 LQENEKIHRELQDKLATAKKHQVFVTETYENNMIELKLLLD 214
Cdd:COG1196 427 EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
44-416 |
4.65e-05 |
|
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: 48.12 E-value: 4.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 44 LEYSAEQEERLKKELEAATDRIKQLEEN---FEAERAAHLKSKFNlEITqmriRELEGALQMEKVSQAEALSDLEMIRKE 120
Cdd:TIGR01612 2257 LHNNKIQIIYFNSELHKSIESIKKLYKKinaFKLLNISHINEKYF-DIS----KEFDNIIQLQKHKLTENLNDLKEIDQY 2331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 121 FKEVENAYERE-KQKAQENLEKVNRLEREYISTNKQMNEKIEEKKEIIKDLSERLQENEKIHRELQDKLatakkhqVFVT 199
Cdd:TIGR01612 2332 ISDKKNIFLHAlNENTNFNFNALKEIYDDIINRENKADEIENINNKENENIMQYIDTITKLTEKIQDIL-------IFVT 2404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 200 eTYENNMIELKLLLdsfamsgqrtagtcKDKDKPSSLSVLETLRYTLTAYQ---NKLEDTSNELKKMNALCENTTKELEI 276
Cdd:TIGR01612 2405 -TYENDNNIIKQHI--------------QDNDENDVSKIKDNLKKTIQSFQeilNKIDEIKAQFYGGNNINNIIITISQN 2469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 277 SRDKMCVLSQDLK------EARDKLANANKELNHLHTECADK--AALIGTLQMELQNVQQR-WEEEKVRAAESENEIQKL 347
Cdd:TIGR01612 2470 ANDVKNHFSKDLTieneliQIQKRLEDIKNAAHEIRSEQITKytNAIHNHIEEQFKKIENNsNKDEVYKINEIDNIIEKI 2549
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024433733 348 tRAYKKDMEEKLTFLHGlYQHLVAGCV--------LIKQPEGILDRFSWsELCAVLQENVDALILDLNRANEKISHL 416
Cdd:TIGR01612 2550 -INYNKEPEVKLHAIID-NKNEFASIIpdiknliaLIESEYGNNNNISY-KVAIKHEEDANNIILDLNKSQNILNHL 2623
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
752-962 |
4.84e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 4.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 752 CDRRPIMKSIASLQKQIAEFTQRLHTVEVERCSLR--RELAEFKLNFSKMKQEADKAQSLKEQLSLFKQSKLIAhkRFES 829
Cdd:COG4913 218 LEEPDTFEAADALVEHFDDLERAHEALEDAREQIEllEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLE--LLEA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 830 ACEELNNALHwehQAQVLLNEQAQQLQELNNKLELHsseeadKNQVLSETVKRLSEAKMELRRKDQSLRQLNRLLTQLEQ 909
Cdd:COG4913 296 ELEELRAELA---RLEAELERLEARLDALREELDEL------EAQIRGNGGDRLEQLEREIERLERELEERERRRARLEA 366
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2024433733 910 DKRRLKESIHDAESALCMAAKDRELIINQMKSVEATLHTVRDQTLLSWTAATR 962
Cdd:COG4913 367 LLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRR 419
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
745-918 |
4.86e-05 |
|
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: 47.45 E-value: 4.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 745 RALEAGSCDRRPIMKSIASLQKQIAEFTQRLHTVEVERCSLRRELAEFKLNFSKMKQE-ADKAQSLKEQL-SLFKQSKLI 822
Cdd:COG4942 41 KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAElEAQKEELAELLrALYRLGRQP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 823 AHKRFESAcEELNNALHWEHQAQVLLNEQAQQLQELNNKLElhssEEADKNQVLSETVKRLSEAKMELRRKDQSLRQL-- 900
Cdd:COG4942 121 PLALLLSP-EDFLDAVRRLQYLKYLAPARREQAEELRADLA----ELAALRAELEAERAELEALLAELEEERAALEALka 195
|
170 180
....*....|....*....|
gi 2024433733 901 --NRLLTQLEQDKRRLKESI 918
Cdd:COG4942 196 erQKLLARLEKELAELAAEL 215
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
759-916 |
5.07e-05 |
|
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: 47.45 E-value: 5.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 759 KSIASLQKQIAEFTQRLHTVEVERCSLRRELAEFKLNFSKMKQEADKAQSLKEQLSLFKQS-------KLIAHKRFESAC 831
Cdd:COG4942 69 RRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEdfldavrRLQYLKYLAPAR 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 832 EELNNALHWE----HQAQVLLNEQAQQLQELNNKLELH----SSEEADKNQVLSETVKRLSEAKMELRRKDQSLRQLNRL 903
Cdd:COG4942 149 REQAEELRADlaelAALRAELEAERAELEALLAELEEEraalEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
170
....*....|...
gi 2024433733 904 LTQLEQDKRRLKE 916
Cdd:COG4942 229 IARLEAEAAAAAE 241
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
800-968 |
7.81e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.24 E-value: 7.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 800 KQEADKA---QSLKEQLSLFKQSKLIAHKRF------------ESACEELNNALHWEHQAQVLLNEQAQQLQELNNKLEL 864
Cdd:COG1196 206 ERQAEKAeryRELKEELKELEAELLLLKLREleaeleeleaelEELEAELEELEAELAELEAELEELRLELEELELELEE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 865 HSSEEADKNQVLSETVKRLSEAKMELRRKDQSLRQLNRLLTQLEQDKRRLKESIHDAESALCMAAKDRELIINQMKSVEA 944
Cdd:COG1196 286 AQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365
|
170 180
....*....|....*....|....*..
gi 2024433733 945 TLHTV---RDQTLLSWTAATRNDFTLQ 968
Cdd:COG1196 366 ALLEAeaeLAEAEEELEELAEELLEAL 392
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
169-503 |
1.30e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.59 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 169 DLSERLQENEKIHRELQDKLATAKKHQvfvtETYENNMIELKLLLDSfamsgqrtagtcKDKDKPSSLSVLETLRYTLTA 248
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKEL----EELEEELEQLRKELEE------------LSRQISALRKDLARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 249 YQNKLEDTSNELKKMNALCENTTKELEISRDKmcvlsqdLKEARDKLANANKELNHLHTECADKAALIGTLQMELQ---- 324
Cdd:TIGR02168 745 LEERIAQLSKELTELEAEIEELEERLEEAEEE-------LAEAEAEIEELEAQIEQLKEELKALREALDELRAELTllne 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 325 ---NVQQRWEEEKVRAAESENEIQKLTRAyKKDMEEKLTFLHGLYQHLVAGC-VLIKQPEGILDRF-SWSELCAVLQENV 399
Cdd:TIGR02168 818 eaaNLRERLESLERRIAATERRLEDLEEQ-IEELSEDIESLAAEIEELEELIeELESELEALLNERaSLEEALALLRSEL 896
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 400 DALILDLNRANEKISHLEYICKSKSDTMKELQRSQE---------------------DDMSKMAEQMKAQESCWQKQKKY 458
Cdd:TIGR02168 897 EELSEELRELESKRSELRRELEELREKLAQLELRLEglevridnlqerlseeysltlEEAEALENKIEDDEEEARRRLKR 976
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2024433733 459 LEQQYSDlLGEVHARA-QEYKETAEKNKEkicvLEKRQEEL--ALENL 503
Cdd:TIGR02168 977 LENKIKE-LGPVNLAAiEEYEELKERYDF----LTAQKEDLteAKETL 1019
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
761-946 |
1.37e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 761 IASLQKQIAEFTQRLHTVEVERCSLRRELAEFKlNFSKMKQEADKAQSLKEQLSLFKQSKLIAHKR-FESACEELNnalh 839
Cdd:PRK03918 461 LKRIEKELKEIEEKERKLRKELRELEKVLKKES-ELIKLKELAEQLKELEEKLKKYNLEELEKKAEeYEKLKEKLI---- 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 840 wEHQAQVL-LNEQAQQLQELNNKLELHSSEEADKNQVLSETVKRLSEAKM----ELRRKDQSLRQLNRLLTQL---EQDK 911
Cdd:PRK03918 536 -KLKGEIKsLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFesveELEERLKELEPFYNEYLELkdaEKEL 614
|
170 180 190
....*....|....*....|....*....|....*
gi 2024433733 912 RRLKESIHDAESALCMAAKDRELIINQMKSVEATL 946
Cdd:PRK03918 615 EREEKELKKLEEELDKAFEELAETEKRLEELRKEL 649
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
36-515 |
1.53e-04 |
|
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: 46.17 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 36 LLTRQVHKLEYSAEQEERLKKELEAATDRIKQLEENF--EAERAAHLKSKFNleITQMRIRELEGALQMEKVSQAEALSD 113
Cdd:TIGR04523 27 IANKQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLnkDEEKINNSNNKIK--ILEQQIKDLNDKLKKNKDKINKLNSD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 114 LEMIRKEFK---------EVE-NAYEREKQKAQENLEKVN----RLEREYISTNKQMNEKIEEKKEIIKDLSERLQENEK 179
Cdd:TIGR04523 105 LSKINSEIKndkeqknklEVElNKLEKQKKENKKNIDKFLteikKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLN 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 180 IHRELQD--KLATAKKHQVFVTETY--ENNMIELKLLldsfAMSGQRTAGTCKDKDKPSSLSVLETLrytLTAYQNKLED 255
Cdd:TIGR04523 185 IQKNIDKikNKLLKLELLLSNLKKKiqKNKSLESQIS----ELKKQNNQLKDNIEKKQQEINEKTTE---ISNTQTQLNQ 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 256 TSNELKKMNALCENTTKELEISRDKMCVLSQDLKEARDKLANANKElnhlhtecaDKAALIGTLQMELQNVQQRWEEEKV 335
Cdd:TIGR04523 258 LKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQ---------KEQDWNKELKSELKNQEKKLEEIQN 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 336 RAAESENEIQKLTRAYKKDMEEKLTflhglyqhlvagcvliKQPEGildrfswSELCAVLQENVDALILDLNRANEKISH 415
Cdd:TIGR04523 329 QISQNNKIISQLNEQISQLKKELTN----------------SESEN-------SEKQRELEEKQNEIEKLKKENQSYKQE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 416 LEYICKSKSDTMKELQRsQEDDMSKMAEQMKAQescwQKQKKYLEQQYSDLLGEVHARAQEYKETAEKNKEK---ICVLE 492
Cdd:TIGR04523 386 IKNLESQINDLESKIQN-QEKLNQQKDEQIKKL----QQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKeliIKNLD 460
|
490 500 510
....*....|....*....|....*....|
gi 2024433733 493 KRQEEL-----ALENLY--VKNTLTQIQKE 515
Cdd:TIGR04523 461 NTRESLetqlkVLSRSInkIKQNLEQKQKE 490
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
10-195 |
3.21e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.31 E-value: 3.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 10 KKQNSALQNLSKKMKDMELEHRDCSDLLTRQVHKLEYSAEQEERLKKELEAA-------TDRIKQLEE--NFEAERAAHL 80
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAqaeeyelLAELARLEQdiARLEERRREL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 81 KSkfNLEITQMRIRELEGALQMEKVSQAEALSDLEMIRKEFKEVENAYEREKQKAQENLEKVNRLEREYISTNKQMNEKI 160
Cdd:COG1196 315 EE--RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
170 180 190
....*....|....*....|....*....|....*
gi 2024433733 161 EEKKEIIKDLSERLQENEKIHRELQDKLATAKKHQ 195
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELE 427
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
789-946 |
3.98e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.05 E-value: 3.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 789 LAEFKLNFSKMKQEADKAQSLKEQLS-LFKQSKLIAHKRFESACEELNNALHWEHQAQVLLNEQAQQLQELNNKLELH-- 865
Cdd:TIGR02168 195 LNELERQLKSLERQAEKAERYKELKAeLRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELrl 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 866 -----SSEEADKNQVLSETVKRLSEAKMELRRKDQSLRQLNRLLTQLEQDKRRLKESIHDAESALCMAAKDRELIINQMK 940
Cdd:TIGR02168 275 evselEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE 354
|
....*.
gi 2024433733 941 SVEATL 946
Cdd:TIGR02168 355 SLEAEL 360
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
6-339 |
7.32e-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: 44.34 E-value: 7.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 6 LQSCKKQ-NSALQNLSKKMKDMELEHRDCSDLLTR-------------QVHKLEYSAEQEERLKKELEAATDRIKQLEEN 71
Cdd:pfam15921 470 LESTKEMlRKVVEELTAKKMTLESSERTVSDLTASlqekeraieatnaEITKLRSRVDLKLQELQHLKNEGDHLRNVQTE 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 72 FEAERAAHLKSKFNLEITQMRIREL----------EGALQMEKVSQAEALSDLEMIRKEFKEVEnayEREKQKAQENLEK 141
Cdd:pfam15921 550 CEALKLQMAEKDKVIEILRQQIENMtqlvgqhgrtAGAMQVEKAQLEKEINDRRLELQEFKILK---DKKDAKIRELEAR 626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 142 VNRLEREYIstnKQMNEKieekkeiikdlSERLQENEKIHRE---LQDKLATAKKHQVFVTETYEnnmielkLLLDSFAM 218
Cdd:pfam15921 627 VSDLELEKV---KLVNAG-----------SERLRAVKDIKQErdqLLNEVKTSRNELNSLSEDYE-------VLKRNFRN 685
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 219 SGQRTAGTCKdkdkpsslsvleTLRYTLTAYQNKLEDTSNELKKMNA-------LCENTTKELEISRDKMCVLSQDLKEA 291
Cdd:pfam15921 686 KSEEMETTTN------------KLKMQLKSAQSELEQTRNTLKSMEGsdghamkVAMGMQKQITAKRGQIDALQSKIQFL 753
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2024433733 292 RDKLANANKELNHLHTECADKAALIGTL---------QMELQNVQQRWEEEKVRAAE 339
Cdd:pfam15921 754 EEAMTNANKEKHFLKEEKNKLSQELSTVateknkmagELEVLRSQERRLKEKVANME 810
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
16-344 |
7.48e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 7.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 16 LQNLSKKMKDMELEHRDCSDLLTRQVHKLEYSAEQEERLKKELEAATDRIKQL--EENFEAERAAHLKSKfnLEITQMRI 93
Cdd:PTZ00121 1600 LYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELkkAEEENKIKAAEEAKK--AEEDKKKA 1677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 94 RELEGAlQMEKVSQAEALSDLEMIRKEFKEVENAYEREKQKAqenlEKVNRLEREYISTNKQMNEKIEEKKEIIKDLSER 173
Cdd:PTZ00121 1678 EEAKKA-EEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKA----EELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD 1752
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 174 LQENEKIHrelQDKLATAKKHQVFVTEtyENNMIELKLlldsfamsgqrtagtcKDKDKPSSLSVLETLRYTLTAYQNKL 253
Cdd:PTZ00121 1753 EEEKKKIA---HLKKEEEKKAEEIRKE--KEAVIEEEL----------------DEEDEKRRMEVDKKIKDIFDNFANII 1811
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 254 EDTsnelkKMNALCENTTKELEISRDKMCVLSQDL-----KEARDKLANANKELNHLHTECADKAALIGTLQMELQNVQQ 328
Cdd:PTZ00121 1812 EGG-----KEGNLVINDSKEMEDSAIKEVADSKNMqleeaDAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEE 1886
|
330
....*....|....*.
gi 2024433733 329 RWEEEKVRAAESENEI 344
Cdd:PTZ00121 1887 ADEIEKIDKDDIEREI 1902
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
51-918 |
7.69e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 44.19 E-value: 7.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 51 EERLKKELEAATDRIKQLEEnfeaERAAHLKSKF-NLEITQMRIRELEGALQMEKvsqaealsdlemirkefKEVENAYE 129
Cdd:pfam02463 153 ERRLEIEEEAAGSRLKRKKK----EALKKLIEETeNLAELIIDLEELKLQELKLK-----------------EQAKKALE 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 130 REKQKAQEnlekvnRLEREYISTNKQMNEKIEEKKEIIKDLSERLQENEKIHRELQDKLATAKKHQVFVTEtyENNMIEL 209
Cdd:pfam02463 212 YYQLKEKL------ELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKE--EEKEKKL 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 210 KLLLDSFAMSGQRTAGTCKDKDKPSSLSVLETLRYTLTAYQNKLEDTSNELKKMNALcENTTKELEISRDKMCVLSQDLK 289
Cdd:pfam02463 284 QEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEEL-EKELKELEIKREAEEEEEEELE 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 290 EARDKLANA---NKELNHLHTECADKAALIGTLQMELQNVQQRWEEEKVRAAESENEIQKLTRAYKKDMEEKLTflhgly 366
Cdd:pfam02463 363 KLQEKLEQLeeeLLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEE------ 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 367 qhlvagcvlikqpEGILDRFSWSELCAVLQENVDALILDLNRANEKISHLEYICKSKSDTMKELQRSQEDDMSKMAEQMK 446
Cdd:pfam02463 437 -------------ESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKES 503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 447 AQESCWQKQKKYLEQQYSDLLGEVHARAQEYKETAEKNKEKICVLEkrqeelALENLYVKNTLTQIQKEHSSLLAACALL 526
Cdd:pfam02463 504 KARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAV------IVEVSATADEVEERQKLVRALTELPLGA 577
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 527 AGALYPLygrscaMSIQRDLLQDQVNIYELVNQEIRTLVHILSGVEEEkeddakikkhKFRGLIHVFRRGVIAVLAANRL 606
Cdd:pfam02463 578 RKLRLLI------PKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDD----------KRAKVVEGILKDTELTKLKESA 641
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 607 KVLAQSSSSLFSLINGFKEGIGILVCVGDSKGKHNMSRYNKEGIRCVEALNWFTSPDLLTAVISSVTE-------LQDVI 679
Cdd:pfam02463 642 KAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKeelkklkLEAEE 721
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 680 SKTDPKSCLSGRLLVSAARNsfskLMDKLNVIMESVPLDSSRSVTYVEKNSLIQRLAHglhrinaraleagscdrrpimk 759
Cdd:pfam02463 722 LLADRVQEAQDKINEELKLL----KQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKE---------------------- 775
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 760 siasLQKQIAEFTQRLHTVEVERCSLRRELAEFKLNFSKMKQEADKAQSLKEQLSLFKQSKLIAHKRFESACEELNNALH 839
Cdd:pfam02463 776 ----LAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKL 851
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024433733 840 WEHQAQVLLNEQAQQLQELNNKLELHSSEEADKnqvlsetVKRLSEAKMELRRKDQSLRQLNRLLTQLEQDKRRLKESI 918
Cdd:pfam02463 852 AEEELERLEEEITKEELLQELLLKEEELEEQKL-------KDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERI 923
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
37-497 |
1.37e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 37 LTRQVHKLEYSAEQEERLKKELEAATDRIKQLEENFEAERAAHLKSKFNLEITQMR--IRELEGALQMEKVSQAEALSDL 114
Cdd:PTZ00121 1099 KAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVeiARKAEDARKAEEARKAEDAKKA 1178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 115 EMIRKEfKEVENAYEREKQKAQENLEKVNRLEREyistnkqmnekieekkeIIKDLSERLQENEKIHRELQDKLATAKKH 194
Cdd:PTZ00121 1179 EAARKA-EEVRKAEELRKAEDARKAEAARKAEEE-----------------RKAEEARKAEDAKKAEAVKKAEEAKKDAE 1240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 195 QVFVTETYENNMIELKLLLDSFAMSGQRTAGT-CKDKDKPSSLSVLETLRYTLTAYQNKLEDTSNELKKMnalCENTTKE 273
Cdd:PTZ00121 1241 EAKKAEEERNNEEIRKFEEARMAHFARRQAAIkAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKK---AEEAKKA 1317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 274 LEisrdkmcvLSQDLKEARDKLANANKElnhlhTECADKAALIGTLQMELQNVQQRWEEEKVRAAE-SENEIQKLTRAYK 352
Cdd:PTZ00121 1318 DE--------AKKKAEEAKKKADAAKKK-----AEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEkKKEEAKKKADAAK 1384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 353 KDMEEKltflhglyqhlvagcvliKQPEGILDRfswSELCAVLQENVDALILDLNRANEKISHLEYICKSKSDTMKELQR 432
Cdd:PTZ00121 1385 KKAEEK------------------KKADEAKKK---AEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEA 1443
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024433733 433 SQEDDMSKMAEQMKAQESCWQKQKKYLEQQYSDLLGEVHARAQEYKETAEKNKEKICVLEKRQEE 497
Cdd:PTZ00121 1444 KKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEA 1508
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
6-348 |
1.61e-03 |
|
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: 42.79 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 6 LQSCKKQNsalqnlskKMKDMEL---EHRDCSDLLTR----QVHKLEYSAEQEERLKKELE------------------- 59
Cdd:pfam05483 247 IQITEKEN--------KMKDLTFlleESRDKANQLEEktklQDENLKELIEKKDHLTKELEdikmslqrsmstqkaleed 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 60 --AATDRIKQLEENFEAE-------RAAHLKSKFNLEITQMRIRELEGALQMEKVSQAEALSDLEM-IRKEFKEVE--NA 127
Cdd:pfam05483 319 lqIATKTICQLTEEKEAQmeelnkaKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMeLQKKSSELEemTK 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 128 YEREKQKAQENLEKVNRLEREYISTNKQMNEKIEEKKEIIKDLSERLQENEKIHRELQDKLATAKKHQVFVTETYENNMI 207
Cdd:pfam05483 399 FKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKT 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 208 EL---------------KLLLDSFAMSG------------QRTAGTCKdKDKPSSLSVLETLRYTLTAYQNKLEDTSNEL 260
Cdd:pfam05483 479 ELekeklknieltahcdKLLLENKELTQeasdmtlelkkhQEDIINCK-KQEERMLKQIENLEEKEMNLRDELESVREEF 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 261 K--------KMNALCENTTK---ELEISRDKMCVLSQDLKEARDKLANANKELNHLHTE--------CADKAAL------ 315
Cdd:pfam05483 558 IqkgdevkcKLDKSEENARSieyEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQEnkalkkkgSAENKQLnayeik 637
|
410 420 430
....*....|....*....|....*....|...
gi 2024433733 316 IGTLQMELQNVQQRWeEEKVRAAESENEIQKLT 348
Cdd:pfam05483 638 VNKLELELASAKQKF-EEIIDNYQKEIEDKKIS 669
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
764-945 |
1.90e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 42.76 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 764 LQKQIAEFTQRLHTVEVERCslrrelaEFKLNFSKMKQEADKAQSLKEQLSLFKQSKliahkrfesacEELNNaLHWEHQ 843
Cdd:COG5022 904 LESEIIELKKSLSSDLIENL-------EFKTELIARLKKLLNNIDLEEGPSIEYVKL-----------PELNK-LHEVES 964
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 844 AqvlLNEQAQQLQELNNKLELHSSEEADKNQVLSETVKRL---SEAKMELRRKDQSLRQLNRLLTQLEQDKRRLKeSIHD 920
Cdd:COG5022 965 K---LKETSEEYEDLLKKSTILVREGNKANSELKNFKKELaelSKQYGALQESTKQLKELPVEVAELQSASKIIS-SEST 1040
|
170 180
....*....|....*....|....*
gi 2024433733 921 AESALcmaAKDRELIINQMKSVEAT 945
Cdd:COG5022 1041 ELSIL---KPLQKLKGLLLLENNQL 1062
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
14-359 |
1.92e-03 |
|
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: 42.70 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 14 SALQNLSKKMKDMELEHRDcsdlLTRQVHKLEYSAEQE----ERLKKELEAATDRIKQLEEnfEAERAAHLKSKFNLEIT 89
Cdd:TIGR04523 204 SNLKKKIQKNKSLESQISE----LKKQNNQLKDNIEKKqqeiNEKTTEISNTQTQLNQLKD--EQNKIKKQLSEKQKELE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 90 QM--RIRELEGALQ--------MEKVSQAEALSDLemiRKEFKEVENAYEREKQKAQENLEKVNRLEREYISTNKQMNEK 159
Cdd:TIGR04523 278 QNnkKIKELEKQLNqlkseisdLNNQKEQDWNKEL---KSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNS 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 160 IEEKKEIIKDLSERLQENEKIHRELQDKLATAK--KHQVFVTETYENNMIELKLLLDSfamsgqrtagtcKDKDKPSSLS 237
Cdd:TIGR04523 355 ESENSEKQRELEEKQNEIEKLKKENQSYKQEIKnlESQINDLESKIQNQEKLNQQKDE------------QIKKLQQEKE 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 238 VLETLRYTLTAYQNKLEDTSNELKKMNALCENTTKELEISRDKmcvLSQDLKEARDKLANANKELNHLHTECADKAALIG 317
Cdd:TIGR04523 423 LLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRES---LETQLKVLSRSINKIKQNLEQKQKELKSKEKELK 499
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2024433733 318 TLQMELQNVQQRWEEEKVRAAESENEIQKLTrAYKKDMEEKL 359
Cdd:TIGR04523 500 KLNEEKKELEEKVKDLTKKISSLKEKIEKLE-SEKKEKESKI 540
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
3-149 |
2.28e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 3 ETSLQSCKKQNSALQNLSKKMKDMElehrDCSDLLTRQVHKLEYSAEQEERLKKELEAATDRIKQLEENFEAERAAHLKS 82
Cdd:PRK02224 578 NSKLAELKERIESLERIRTLLAAIA----DAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIEEARE 653
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024433733 83 KfnLEITQMRIRELEGALQMEKVSQAEALSDLEMIRKEFKEVENAyeREKQKAQENleKVNRLEREY 149
Cdd:PRK02224 654 D--KERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEEL--RERREALEN--RVEALEALY 714
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
759-918 |
2.30e-03 |
|
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: 41.45 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 759 KSIASLQKQIAEFTQRLHTVEVERCSLRRELAEFKlnfSKMKQEADKAQSLKEQLSLFKQSKliahkrfesaceELNNAL 838
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLE---LEIEEVEARIKKYEEQLGNVRNNK------------EYEALQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 839 HWEHQAQVLLNEQAQQLQELNNKLELHSSEEADKNQVLSETVKRLSEAKMELrrkDQSLRQLNRLLTQLEQDKRRLKESI 918
Cdd:COG1579 96 KEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEL---DEELAELEAELEELEAEREELAAKI 172
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
16-305 |
2.82e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 16 LQNLSKKMKDMELEHRDcsdlLTRQVHKLEYSAEQEERLKKELEAAtDRIKQLEENFEAERAAHLKSKFN-LEITQMRIR 94
Cdd:PRK03918 461 LKRIEKELKEIEEKERK----LRKELRELEKVLKKESELIKLKELA-EQLKELEEKLKKYNLEELEKKAEeYEKLKEKLI 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 95 ELEGalqmEKVSQAEALSDLEMIRKEFKEVEnayeREKQKAQENLEKV-NRLEREYISTNKqmnekieekkeiikDLSER 173
Cdd:PRK03918 536 KLKG----EIKSLKKELEKLEELKKKLAELE----KKLDELEEELAELlKELEELGFESVE--------------ELEER 593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 174 LQENEKIHRELQdKLATAKKHqvfvtetYENNMIELKLLLDSFAMSGQRTAGTCKD-KDKPSSLSVLETlRYTLTAYQNK 252
Cdd:PRK03918 594 LKELEPFYNEYL-ELKDAEKE-------LEREEKELKKLEEELDKAFEELAETEKRlEELRKELEELEK-KYSEEEYEEL 664
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2024433733 253 LEDTSnELKKMNALCENTTKELEISRDKMCVLSQDLKEARDKLANANKELNHL 305
Cdd:PRK03918 665 REEYL-ELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKL 716
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
766-922 |
2.89e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 766 KQIAEFTQRLHTVEVERCSLRRELAEFKLNFSKMKQEADKAQSLKEQLSLFKQSKLIAHK------RFESACEELNNALH 839
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAElaelpeRLEELEERLEELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 840 WEHQAQVLLNEQAQQLQELNNKLELHSSEEADKNQVLSETVKRLSEAKMELRRKdqsLRQLNRLLTQLEQDKRRLKESIH 919
Cdd:COG4717 161 LEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEE---LEEAQEELEELEEELEQLENELE 237
|
...
gi 2024433733 920 DAE 922
Cdd:COG4717 238 AAA 240
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
14-189 |
2.99e-03 |
|
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: 42.04 E-value: 2.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 14 SALQNLSKKMKDMELEHRDCSDLLTRQVHKLEYSAEQEERLKKELEAatdRIKQLEENfEAERAAHLKSKFNLEITQMRI 93
Cdd:pfam05557 9 ARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQK---RIRLLEKR-EAEAEEALREQAELNRLKKKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 94 RELEGALQMEKVSQAEALSDLEM-IRKEFKEVENAYEREKQKAQENLEKVNRLEREYISTNKQMNEKIEEKKEIIKDLSE 172
Cdd:pfam05557 85 LEALNKKLNEKESQLADAREVIScLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSS 164
|
170
....*....|....*..
gi 2024433733 173 RLQENEKIhRELQDKLA 189
Cdd:pfam05557 165 LAEAEQRI-KELEFEIQ 180
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
279-487 |
3.16e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 3.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 279 DKMCVLSQDLKEARDKLANANKELNHLHTECADKAALIGTLQMELQNVQQRWEEEKVRAAESENEIQKLTRAYKKdmeek 358
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 359 ltFLHGLYQHLVAGCVL-----IKQPEGILDRFSwseLCAVLQENVDALILDLNRANEKISHLeyicKSKSDTMKELQRS 433
Cdd:COG3883 91 --RARALYRSGGSVSYLdvllgSESFSDFLDRLS---ALSKIADADADLLEELKADKAELEAK----KAELEAKLAELEA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2024433733 434 QEDDMSKMAEQMKAQESCWQKQKKYLEQQYSDLLGEVHARAQEYKETAEKNKEK 487
Cdd:COG3883 162 LKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
246-584 |
3.32e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.81 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 246 LTAYQNKLEDTSNELKKMNALCENTTKELEISRDKMCVLSQDLKEARDKLANANKELNHLHTECADkaaligtlQMELQN 325
Cdd:PRK01156 178 LRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNE--------LSSLED 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 326 VQQRWEEEkVRAAESENEIQKLTRAYKKDMEEKltflhglYQHLVAGCVLIKQPEgILDRFSWSELCAVLQENVDALILD 405
Cdd:PRK01156 250 MKNRYESE-IKTAESDLSMELEKNNYYKELEER-------HMKIINDPVYKNRNY-INDYFKYKNDIENKKQILSNIDAE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 406 LNRANEKISHLEYICKSKSDTMKelQRSQEDDMSKMAEQMKAQESCWQ------KQKKYLEQQYSDLLGEVHARAQEYKE 479
Cdd:PRK01156 321 INKYHAIIKKLSVLQKDYNDYIK--KKSRYDDLNNQILELEGYEMDYNsylksiESLKKKIEEYSKNIERMSAFISEILK 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 480 TAEKNKEKIcvlEKRQEELALENLYVKNTLTQIQKEHSSLLAACALLAGALYPLYGRS----CAMSIQRDLLQDQVNIY- 554
Cdd:PRK01156 399 IQEIDPDAI---KKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSvcpvCGTTLGEEKSNHIINHYn 475
|
330 340 350
....*....|....*....|....*....|...
gi 2024433733 555 ---ELVNQEIRTLVHILSGVEEEKEDDAKIKKH 584
Cdd:PRK01156 476 ekkSRLEEKIREIEIEVKDIDEKIVDLKKRKEY 508
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
43-497 |
3.43e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.05 E-value: 3.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 43 KLEYSAEQEERLKKELEAATDRIKQLEENFEAERAAHLKSKFNLEITQMRIRELEGALQMEKVSQAEALSDLEMIRKEfk 122
Cdd:PTZ00121 1337 KAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAA-- 1414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 123 EVENAYEREKQKAQEnLEKVNRLEREYISTNKQMNEKIEEKKEIIKDLSERLQENEKIHRELQDKLATAKKHQvfvtety 202
Cdd:PTZ00121 1415 AAKKKADEAKKKAEE-KKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKAD------- 1486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 203 ennmiELKLLLDSFAMSGQRTAGTCKDKDKPSSLSVLETLRYTLTAYQNKLEDTSNELKKmnalCENTTKELEISRDKMC 282
Cdd:PTZ00121 1487 -----EAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKK----AEEKKKADELKKAEEL 1557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 283 VLSQDLKEARD-KLANANKELNHLHTECADKAAligtlQMELQNVQQRWEEEKVRAAES---ENEIQKLTRAYKKDMEEK 358
Cdd:PTZ00121 1558 KKAEEKKKAEEaKKAEEDKNMALRKAEEAKKAE-----EARIEEVMKLYEEEKKMKAEEakkAEEAKIKAEELKKAEEEK 1632
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 359 ltflhglyqhlvagcvliKQPEGILDRFSwselcavlQENVDALILDLNRANEKISHLEYICKSKSDTMK-ELQRSQEDD 437
Cdd:PTZ00121 1633 ------------------KKVEQLKKKEA--------EEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKaEEAKKAEED 1686
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 438 MSKMAEQMKAQEscwqKQKKYLEQQYSDLLGEVHaRAQEYKETAEKNKEKICVLEKRQEE 497
Cdd:PTZ00121 1687 EKKAAEALKKEA----EEAKKAEELKKKEAEEKK-KAEELKKAEEENKIKAEEAKKEAEE 1741
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
6-186 |
4.10e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 4.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 6 LQSCKKQNSALQNLSKKMKDMELEHRDCSDLLTRQVHKLEysaeqeERLKKELEAATDRIKQLEEnFEAERAAHLKSKFN 85
Cdd:PRK03918 541 IKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELE------ELGFESVEELEERLKELEP-FYNEYLELKDAEKE 613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 86 LEITQMRIRELEGALQMEKVSQAEALSDLEMIRKEFKEVENAYEREKQKAQEnlEKVNRLEREYISTN---KQMNEKIEE 162
Cdd:PRK03918 614 LEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELR--EEYLELSRELAGLRaelEELEKRREE 691
|
170 180
....*....|....*....|....
gi 2024433733 163 KKEIIKDLSERLQENEKIHRELQD 186
Cdd:PRK03918 692 IKKTLEKLKEELEEREKAKKELEK 715
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
10-515 |
4.39e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.43 E-value: 4.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 10 KKQNSALQNLSKKMKDMELEHRDcsdlLTRQVHKLEYSAEQEERLKKELEAATDRIKQLEEnfeaeraahLKSKFNLEIt 89
Cdd:PRK01156 193 KSSNLELENIKKQIADDEKSHSI----TLKEIERLSIEYNNAMDDYNNLKSALNELSSLED---------MKNRYESEI- 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 90 qmriRELEGALQMEkvsqaealsdlEMIRKEFKEVENAYER-EKQKAQENLEKVNrlerEYISTNKQMnekiEEKKEIIK 168
Cdd:PRK01156 259 ----KTAESDLSME-----------LEKNNYYKELEERHMKiINDPVYKNRNYIN----DYFKYKNDI----ENKKQILS 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 169 DLSERLQENEKIHRELQDklatakkhqvfvTETYENNMIELKllldsfamsgqrtagtcKDKDKpsslsvLETLRYTLTA 248
Cdd:PRK01156 316 NIDAEINKYHAIIKKLSV------------LQKDYNDYIKKK-----------------SRYDD------LNNQILELEG 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 249 YQNKLEDTSNELKKMNALCENTTKELEISRDKmcvLSQDLKEARDKLANANKELNHLHTECADKAALIGTLQMELQNVQQ 328
Cdd:PRK01156 361 YEMDYNSYLKSIESLKKKIEEYSKNIERMSAF---ISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRE 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 329 RWEEekvraaeseneiqkltraykkdMEEKLTFLHGLYQHLVAGCVLikQPEGILD-RFSWSELCAVLQENVDALILDLN 407
Cdd:PRK01156 438 NLDE----------------------LSRNMEMLNGQSVCPVCGTTL--GEEKSNHiINHYNEKKSRLEEKIREIEIEVK 493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 408 RANEKISHL----EYICKSK-------SDTMKELQRSQEDDMSKMAEQMKAQESCWQKQKKY-------LEQQYSDLLGE 469
Cdd:PRK01156 494 DIDEKIVDLkkrkEYLESEEinksineYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYkslkledLDSKRTSWLNA 573
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 2024433733 470 VHARAQEYKETAEKNKE----KICVLEKRQEELALE----NLYVKNTLTQIQKE 515
Cdd:PRK01156 574 LAVISLIDIETNRSRSNeikkQLNDLESRLQEIEIGfpddKSYIDKSIREIENE 627
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
772-952 |
5.46e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 5.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 772 TQRLHTVEVERCSLRRELAEFklnfskmKQEADKAQSLKEQLslfkQSKLIAHKRFESACEELNNAlhWEHQAQVL-LNE 850
Cdd:COG4913 609 RAKLAALEAELAELEEELAEA-------EERLEALEAELDAL----QERREALQRLAEYSWDEIDV--ASAEREIAeLEA 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 851 QAQQLQELNNKLELHSSEEADKNQVLSETVKRLSEAKMELRRKDQSLRQLNRLLTQLEQDKRRLKESIHDAESALCMAAK 930
Cdd:COG4913 676 ELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERF 755
|
170 180
....*....|....*....|..
gi 2024433733 931 DRELIINQMKSVEATLHTVRDQ 952
Cdd:COG4913 756 AAALGDAVERELRENLEERIDA 777
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
757-913 |
6.19e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 40.78 E-value: 6.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 757 IMKSIASLQKQIAEFTQRLHTVEVERCSLRRELAEFKLNFSKMKQEADKAQSLKEQLSLFKqsKLIAhkrfESACEELNN 836
Cdd:pfam05667 347 LESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQYKVKKKTLDLLPDAEENIAKLQ--ALVD----ASAQRLVEL 420
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024433733 837 ALHWEhQAQVLLNEQAQQLQELNNKLELHSSEEADKNQVLSETVKRLSEakmELRRKDQSLRQLNRLLTQLEQDKRR 913
Cdd:pfam05667 421 AGQWE-KHRVPLIEEYRALKEAKSNKEDESQRKLEEIKELREKIKEVAE---EAKQKEELYKQLVAEYERLPKDVSR 493
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
757-916 |
6.87e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 6.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 757 IMKSIASLQKQIAEFTQRLHTVEVERCSLRRELAEFKLNFSKMKQEADKAQSLKEQLSLFKQSKliahKRFESACEELNN 836
Cdd:PRK03918 191 IEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSK----RKLEEKIRELEE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 837 ALHWEHQAQVLLNEQAQQLQELNNKLELHSSeeadKNQVLSETVKRLSEAKMELRRKDQSLRQLNRLLTQLEQDKRRLKE 916
Cdd:PRK03918 267 RIEELKKEIEELEEKVKELKELKEKAEEYIK----LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEE 342
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
41-357 |
7.15e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.82 E-value: 7.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 41 VHKLEYSAEQEERLKKELEAATDRIKQLEEnfeaeraahLKSKFNLEITQMRIRELEGALQMEKVSQAEALSDLEMIRKE 120
Cdd:TIGR02169 229 LKEKEALERQKEAIERQLASLEEELEKLTE---------EISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGEL 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 121 FKEVENA------YEREKQKAQENLEKvnrLEREYISTNKQMnekieekkeiiKDLSERLQENEKIHRELQDKLATAKkh 194
Cdd:TIGR02169 300 EAEIASLersiaeKERELEDAEERLAK---LEAEIDKLLAEI-----------EELEREIEEERKRRDKLTEEYAELK-- 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 195 qvfvtETYENNMIELKLLLDSFAmsgqrtagtckdkdkpsslsvleTLRYTLTAYQNKLEDTSNElkkMNALCENTTKEL 274
Cdd:TIGR02169 364 -----EELEDLRAELEEVDKEFA-----------------------ETRDELKDYREKLEKLKRE---INELKRELDRLQ 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 275 EISRDkmcvLSQDLKEARDKLANANKELNHLHTECADKAALIGTLQMELQNVQQRWEEEKVRAAESENEIQKLTRAYKKD 354
Cdd:TIGR02169 413 EELQR----LSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKL 488
|
...
gi 2024433733 355 MEE 357
Cdd:TIGR02169 489 QRE 491
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
753-944 |
8.92e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 40.73 E-value: 8.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 753 DRRPIMKSIASLQKQIAEFTQRLHTVEVERCSLRRELAEFKLN----FSKMKQEADKAQSLKEQLSLFKQSKLIAHKRFE 828
Cdd:pfam02463 153 ERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELklqeLKLKEQAKKALEYYQLKEKLELEEEYLLYLDYL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 829 SACEELNNALHWEHQAQVLLNEQAQQLQELNNKLELHSSEEADKNQVLSETVKRLSEAKMELRRKDQSLRQLNRLLTQLE 908
Cdd:pfam02463 233 KLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDD 312
|
170 180 190
....*....|....*....|....*....|....*..
gi 2024433733 909 QDK-RRLKESIHDAESALCMAAKDRELIINQMKSVEA 944
Cdd:pfam02463 313 EEKlKESEKEKKKAEKELKKEKEEIEELEKELKELEI 349
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
758-922 |
9.09e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 9.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 758 MKSIASLQKQIAEFTQRLHTVEVERCSLRRELAEfkLNFSKMKQEADKAQSLKE------QLSLFKQSKLIAHKRFESAC 831
Cdd:PRK03918 548 LEKLEELKKKLAELEKKLDELEEELAELLKELEE--LGFESVEELEERLKELEPfyneylELKDAEKELEREEKELKKLE 625
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024433733 832 EELNNALhwehqaqvllneqaQQLQELNNKLELHSSEEADKNQVLS-ETVKRLSEAKMELRrkdqslRQLNRLLTQLEQD 910
Cdd:PRK03918 626 EELDKAF--------------EELAETEKRLEELRKELEELEKKYSeEEYEELREEYLELS------RELAGLRAELEEL 685
|
170
....*....|..
gi 2024433733 911 KRRLKESIHDAE 922
Cdd:PRK03918 686 EKRREEIKKTLE 697
|
|
| |
