|
Name |
Accession |
Description |
Interval |
E-value |
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
132-685 |
8.49e-34 |
|
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: 138.33 E-value: 8.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 132 PSTNASRLYRDRGPYSTALQGSMhPTLTPEVlqstdpSGAHPGATMSEDEFMHQLMRLVKaHQVAYNGIQEGNTAwttgS 211
Cdd:pfam17380 227 PHTLAPYEKMERRKESFNLAEDV-TTMTPEY------TVRYNGQTMTENEFLNQLLHIVQ-HQKAVSERQQQEKF----E 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 212 KSFQGEVMQEKNSYVGDQSDILK-HTNEIEKQFELER---VRLEKQRREQQIEREFEERQLKEKERiERQRNVVKEIERE 287
Cdd:pfam17380 295 KMEQERLRQEKEEKAREVERRRKlEEAEKARQAEMDRqaaIYAEQERMAMERERELERIRQEERKR-ELERIRQEEIAME 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 288 AEERRRREREWLEKQRKKALHLQEMQAKAREEFERRQQLAAQLVQqqREEREKLEKQQEQARlalekkrreeEELQKRQQ 367
Cdd:pfam17380 374 ISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQ--KVEMEQIRAEQEEAR----------QREVRRLE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 368 AERQIEEMKEKEKRKKLEEQRERGRQLMEKQRKEK-ELQKKQNIAREMKEMQRK--QKENEERLWEIVRQTEARQQKEKD 444
Cdd:pfam17380 442 EERAREMERVRLEEQERQQQVERLRQQEEERKRKKlELEKEKRDRKRAEEQRRKilEKELEERKQAMIEEERKRKLLEKE 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 445 EHLRLQQLArefeerkrkeeeallktqqEEEDRKEeallkiqQEEEDRKEQAKNEAERIrQEGERRQSEEMMRIEAANRI 524
Cdd:pfam17380 522 MEERQKAIY-------------------EEERRRE-------AEEERRKQQEMEERRRI-QEQMRKATEERSRLEAMERE 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 525 RAMGSgNLLPAMSSRGSSGDNGHAHTFHPEAtdfpgRVDFQTSQTLPVDPNVIHFTaapstvpSAVPAWVrgpqpwrlPP 604
Cdd:pfam17380 575 REMMR-QIVESEKARAEYEATTPITTIKPIY-----RPRISEYQPPDVESHMIRFT-------TQSPEWA--------TP 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 605 DPNTNQPEWFEPSTTETPTRIL---SGCVPEGDCNFSYDQDLLCPHPSDSSRYLQCTPMIGRRGRWTERNCPPTLVFLHA 681
Cdd:pfam17380 634 SPATWNPEWNTVTAEEETPGIPiihSQCQVNGECELKYDSDSFCAHPSNPSMYLQCAPLYGRLGRWTERHCPDTLIFIVS 713
|
....
gi 1530640611 682 HAAC 685
Cdd:pfam17380 714 IGRC 717
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
229-520 |
6.13e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 75.95 E-value: 6.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 229 QSDILKHTNEIEKQFELERVRLEKQRREQQIEREFEERQLKE--KERIERQRNVVKEIEREAEERRRREREWLEKQRKKA 306
Cdd:PTZ00121 1445 KADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADeaKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKA 1524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 307 LHLQEMQ-AKAREEFERRQQLAAQLVQQQREEREKLE--KQQEQARLALEKKRREEEELQKRQQAERQIEEMKEKEKRKK 383
Cdd:PTZ00121 1525 DEAKKAEeAKKADEAKKAEEKKKADELKKAEELKKAEekKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEE 1604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 384 LEEQRERGRQLMEKQRKEKELQKKQNIARemKEMQRKQKENEErlweiVRQTEARQQKEKDEHLRLQQLAREFEERKRKE 463
Cdd:PTZ00121 1605 KKMKAEEAKKAEEAKIKAEELKKAEEEKK--KVEQLKKKEAEE-----KKKAEELKKAEEENKIKAAEEAKKAEEDKKKA 1677
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1530640611 464 EEAllKTQQEEEDRKEEALLKIQQEEEDRKEQAKNEAERIRQEGERRQSEEMMRIEA 520
Cdd:PTZ00121 1678 EEA--KKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKA 1732
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
230-514 |
1.91e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.20 E-value: 1.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 230 SDILkhtNEIEKQfeLERvrLEKQRRE----QQIEREFEERQ----LKEKERIERQRNVVKEIEREAEERRRREREWLEK 301
Cdd:COG1196 192 EDIL---GELERQ--LEP--LERQAEKaeryRELKEELKELEaellLLKLRELEAELEELEAELEELEAELEELEAELAE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 302 QRKKALHLQEMQAKAREEFERRQQLAAQLVQQQREEREKLEKQQEQARlalekkrreeEELQKRQQAERQIEEMKEKEKR 381
Cdd:COG1196 265 LEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR----------ELEERLEELEEELAELEEELEE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 382 KKLEEQRERGRQLMEKQRKEKELQKKQNIAREMKEMQRKQKENEERLWEIVRQTEARQQKEKDEHLRLQQLAREFEERKR 461
Cdd:COG1196 335 LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1530640611 462 KEEEALLKTQQEEEDRKEEALLKIQQEEEDRKEQAKNEAERIRQEGERRQSEE 514
Cdd:COG1196 415 RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
234-514 |
1.18e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 71.71 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 234 KHTNEIEKQFELERVRLEKQRREQQIEREFEERQLKEKERIERQRNVVKEIEREAEERRRREREWLEKQRK-----KALH 308
Cdd:PTZ00121 1477 KKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKadelkKAEE 1556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 309 LQEMQAKAREEFERRQQLAAQLVQQQREEREKLEKQQEQARLALEKKRREEEELQKRQQAERQIEEMKEKEKRKKLEEQR 388
Cdd:PTZ00121 1557 LKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVE 1636
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 389 ERGRQLMEKQRKEKELQKKQNIAREMKEMQRKQKENEERLWEIVRQTEARQQKEKDEHLRLQQLAREFEERKRkeeeall 468
Cdd:PTZ00121 1637 QLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKK------- 1709
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1530640611 469 ktQQEEEDRKEEALLKIQQEEEDRKEQAKNEAERIRQEGERRQSEE 514
Cdd:PTZ00121 1710 --KEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDE 1753
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
240-523 |
2.27e-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: 2.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 240 EKQFELERVRLEKQRREQQIER---EFEERQLKEKERIERQRNVVKEIEReaeerrrrerewLEKQRKkalHLQEMQAKA 316
Cdd:COG1196 250 ELEAELEELEAELAELEAELEElrlELEELELELEEAQAEEYELLAELAR------------LEQDIA---RLEERRREL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 317 REEFERRQQLAAQLVQQQREEREKLEKQQEQARLAlekKRREEEELQKRQQAERQIEEMKEKEKRKKLEEQRERGRQLME 396
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEA---EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 397 KQRKEKELQKKQNIAREMKEMQRKQKENEERLWEIVRQTEARQQKEKDEHLRLQQLArefeerkrkeeeallKTQQEEED 476
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA---------------EEEAELEE 456
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1530640611 477 RKEEALLKIQQEEEDRKEQAKNEAERIRQEGERRQSEEMMRIEAANR 523
Cdd:COG1196 457 EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
299-526 |
4.44e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.58 E-value: 4.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 299 LEKQRKKALHLQEMQAKARE-----------EFERRQQLAAQLVQQQREEREKLEKQQEQARLALEKKRreeeelQKRQQ 367
Cdd:COG1196 205 LERQAEKAERYRELKEELKEleaellllklrELEAELEELEAELEELEAELEELEAELAELEAELEELR------LELEE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 368 AERQIEEMKEKEKRKKLEEQRERGRQLMEKQRKEKELQKKQNIAREMKEMQRKQKENEERLweivrQTEARQQKEKDEHL 447
Cdd:COG1196 279 LELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL-----EELEEELEEAEEEL 353
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1530640611 448 RLQQLAREFEERKRKEEEALLKTQQEEEDRKEEALLKIQQEEEDRKEQAKNEAERIRQEGERRQSEEMMRIEAANRIRA 526
Cdd:COG1196 354 EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
240-535 |
9.51e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.42 E-value: 9.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 240 EKQFELERVRLEKQRREQQIEREfEERQLKEKERIERQRNVVKEIEREAEERRRREREWLEKQRKKALHLQEMQAKAREE 319
Cdd:COG1196 285 EAQAEEYELLAELARLEQDIARL-EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 320 FERRQQLAAQLVQQQREEREKLEKQQEQARLALEKKRREEEELQKRQQAERQIEEMKEKEKRKKLEEQRERGRQLMEKQR 399
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 400 KEKELQKKQNIAREMKEMQRKQKENEERLWEIVRQTEARQQKEKDEHLRLQQLAREFEERKRKEEEALLKTQQEEEDRKE 479
Cdd:COG1196 444 LEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLA 523
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1530640611 480 EALLKIQQEEEDRKEQAKNEAERIRQEGERRQSEEMMRIEAANRIRAMGSGNLLPA 535
Cdd:COG1196 524 GAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPL 579
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
234-526 |
3.03e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 67.09 E-value: 3.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 234 KHTNEIEKQFELERVRLEKQRREQQIEREFEERQLKEKERIERQRNVVKEIEREAEERRRREREWLEKQRKKALHLQEMQ 313
Cdd:PTZ00121 1371 KKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAK 1450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 314 AKAREefeRRQQLAAQLVQQQREEREKLEKQQEQARLALEKKRREEEELQKRQQAERQIEEMKEKEKRKKLEEQR--ERG 391
Cdd:PTZ00121 1451 KKAEE---AKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKkaDEA 1527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 392 RQLMEKqRKEKELQKkqniAREMKEMQRKQKENEERLWEIVRQTEARQQKEKDEHLRLQQlAREFEERKRKEEEALLKTQ 471
Cdd:PTZ00121 1528 KKAEEA-KKADEAKK----AEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRK-AEEAKKAEEARIEEVMKLY 1601
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1530640611 472 QEEEDRKEEALLKiQQEEEDRKEQAKNEAE--------RIRQEGERRQSEEMMRIEAANRIRA 526
Cdd:PTZ00121 1602 EEEKKMKAEEAKK-AEEAKIKAEELKKAEEekkkveqlKKKEAEEKKKAEELKKAEEENKIKA 1663
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
229-524 |
3.13e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 64.01 E-value: 3.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 229 QSDILKHTNEIEKQFEL----ERVRLEKQRREQQIEREFEERQLKEKERIERQRNVVKEIEREAEERRRREREWLEKQRK 304
Cdd:PTZ00121 1523 KADEAKKAEEAKKADEAkkaeEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYE 1602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 305 KALHLQEMQAKAREEferrqqlaaqlvqqQREEREKLEKQQEQARLALEKKRREEEELQKRQQAERQieemkekekrkkl 384
Cdd:PTZ00121 1603 EEKKMKAEEAKKAEE--------------AKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKA------------- 1655
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 385 eeQRERGRQLMEKQRKEKELQKKQNIAREMKEMQRKQKENEERLWEIVRQTEARQQKEKDEHLRLQQLAREFEERKRKEE 464
Cdd:PTZ00121 1656 --EEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAE 1733
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1530640611 465 EAllKTQQEEEDRKEEAlLKIQQEEEDRKEQAKNE----AERIRQEGERRQSEEMMRIEAANRI 524
Cdd:PTZ00121 1734 EA--KKEAEEDKKKAEE-AKKDEEEKKKIAHLKKEeekkAEEIRKEKEAVIEEELDEEDEKRRM 1794
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
229-526 |
3.87e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.62 E-value: 3.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 229 QSDILKHTNEIEKQFELERvRLEKQRREQQIEREFEERQlKEKERIERQRNVVKEIEREAEERRRREREWLE--KQRKKA 306
Cdd:PTZ00121 1291 KADEAKKAEEKKKADEAKK-KAEEAKKADEAKKKAEEAK-KKADAAKKKAEEAKKAAEAAKAEAEAAADEAEaaEEKAEA 1368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 307 LHLQEMQAKAREEFERRQQLAAQLVQQQREEREKLEKQQEQARLALEKKRREEEELQKRQQAER---------QIEEMKE 377
Cdd:PTZ00121 1369 AEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKadeakkkaeEAKKADE 1448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 378 KEKRKKLEEQRERGRQLMEKQRKEKELQKKQNIAREMKEMQRKQKENEERLWEIVRQTEARQQKEKDEHLRLQQLAREFE 457
Cdd:PTZ00121 1449 AKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAK 1528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 458 ERKRKEEEALLKTQQE----------EEDRKEEALLKIQQ--EEEDRKEQAKNEAERIRQEGERRQSEEMMRIEAANRIR 525
Cdd:PTZ00121 1529 KAEEAKKADEAKKAEEkkkadelkkaEELKKAEEKKKAEEakKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMK 1608
|
.
gi 1530640611 526 A 526
Cdd:PTZ00121 1609 A 1609
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
215-526 |
5.92e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 62.85 E-value: 5.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 215 QGEVMQEKNSYVGDQSDILKHTNEIEKQFELERVRLEKQRREQQIEREFEE-RQLKEKERIERQRNVVKEIEREAEERRR 293
Cdd:PTZ00121 1392 KADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEaKKADEAKKKAEEAKKAEEAKKKAEEAKK 1471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 294 RERewLEKQRKKALHLQEMQAKAREefERRQQLAAQLVQQQREEREKLEKQQEQARLALEKKRREEEELQKRQQAERQie 373
Cdd:PTZ00121 1472 ADE--AKKKAEEAKKADEAKKKAEE--AKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEK-- 1545
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 374 EMKEKEKRKKLEEQRERGRQLMEKQRKEKELQKKQNIAREMKEMQRKQKENEERLWEIVRQTEARQ-QKEKDEHLRLQQL 452
Cdd:PTZ00121 1546 KKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEaKKAEEAKIKAEEL 1625
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1530640611 453 AREFEERKRKEEealLKTQQEEEDRKEEALLKIQQEEEDRKEQAKNEAERirqegERRQSEEMMRIEAANRIRA 526
Cdd:PTZ00121 1626 KKAEEEKKKVEQ---LKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEE-----DKKKAEEAKKAEEDEKKAA 1691
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
238-523 |
6.39e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 62.85 E-value: 6.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 238 EIEKQFELERvRLEKQRREQQIEREFEERQLKEKERIERQRNVvKEIEREAEERRRREREWLEKQRK-----------KA 306
Cdd:PTZ00121 1119 EAKKKAEDAR-KAEEARKAEDARKAEEARKAEDAKRVEIARKA-EDARKAEEARKAEDAKKAEAARKaeevrkaeelrKA 1196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 307 LHLQEMQAKAREEFERRQQLAAQLVQQQREER----EKLEKQQEQARLALEKKRREEEELQKRQQ----AERQIEEMKEK 378
Cdd:PTZ00121 1197 EDARKAEAARKAEEERKAEEARKAEDAKKAEAvkkaEEAKKDAEEAKKAEEERNNEEIRKFEEARmahfARRQAAIKAEE 1276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 379 EKRKKLEEQRERGRQL-----MEKQRKEKELQKKQNIAREMKEMQRKQKENEERLWEIVRQTEarQQKEKDEHLRLQQLA 453
Cdd:PTZ00121 1277 ARKADELKKAEEKKKAdeakkAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAE--EAKKAAEAAKAEAEA 1354
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 454 REFEERKRKEEEALLKTQQEEEDRKEEALLKiQQEEEDRKEQAKNEAERirqegERRQSEEMMRIEAANR 523
Cdd:PTZ00121 1355 AADEAEAAEEKAEAAEKKKEEAKKKADAAKK-KAEEKKKADEAKKKAEE-----DKKKADELKKAAAAKK 1418
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
215-525 |
1.15e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 62.08 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 215 QGEVMQEKNSYVGDQSDILKHTNEIEKQF-ELERVRLEKQRREQQIEREFEERQLKEKERIERQRNVVKEIEREAeerrr 293
Cdd:PTZ00121 1379 KADAAKKKAEEKKKADEAKKKAEEDKKKAdELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKA----- 1453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 294 rerewleKQRKKAlhlQEMQAKAReefERRQQLAAQLVQQQREEREKLEKQQEQARLALEKKRREEEELQKRQQAERQIE 373
Cdd:PTZ00121 1454 -------EEAKKA---EEAKKKAE---EAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEE 1520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 374 EMKEKEKRKKLEEQRERGRQLMEKQRKEKELQKKQNI--AREMKEMQRKQKENEERLWEIVRQTEARQQKEKdehlRLQQ 451
Cdd:PTZ00121 1521 AKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELkkAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEA----RIEE 1596
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1530640611 452 LAREFEERKRKEEEALLKtqQEEEDRKEEALLKIQQEEEDRKEQAKNEAERIRQEGERRQSEEMMRIEAANRIR 525
Cdd:PTZ00121 1597 VMKLYEEEKKMKAEEAKK--AEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAK 1668
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
246-523 |
3.94e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.15 E-value: 3.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 246 ERVRLEKQRREQQIEREFEERQLKEKERIERQRNVVKEIEREAEERRRREREwleKQRKKALHLQEMQAKAREEFERRQQ 325
Cdd:PTZ00121 1276 EARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEA---KKKADAAKKKAEEAKKAAEAAKAEA 1352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 326 LAAQLVQQQREEREKL-----EKQQEQARLALEKKRREEEELQKRQQAERQIEEMKEKEKRKKLEEQRERGRQLMEKQRK 400
Cdd:PTZ00121 1353 EAAADEAEAAEEKAEAaekkkEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKK 1432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 401 EKELQKKQNIAREMKEMQRKQKEN---EERLWEIVRQTEARQQKEKDEHLRLQQLAREFEERKRKEEEALLKTQQE---- 473
Cdd:PTZ00121 1433 ADEAKKKAEEAKKADEAKKKAEEAkkaEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAkkka 1512
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1530640611 474 ------EEDRKEEALLKIQQE---EEDRKEQAKNEAERIRQEGERRQSEEMMRIEAANR 523
Cdd:PTZ00121 1513 deakkaEEAKKADEAKKAEEAkkaDEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKK 1571
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
217-529 |
5.60e-09 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 59.60 E-value: 5.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 217 EVMQEKNSYVG-DQSDILKHTNEIEKQFELERVRLEKQRREQQIEREFEERQLKEKERIERQrnvvKEIEREAEERRRRE 295
Cdd:pfam02463 202 LKEQAKKALEYyQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKE----EEKLAQVLKENKEE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 296 REWLEKQRKKALHLQEMQAKAREEF---ERRQQLAAQLVQQQREEREKLEKQQEQARLALEKKRREEEELQ-KRQQAERQ 371
Cdd:pfam02463 278 EKEKKLQEEELKLLAKEEEELKSELlklERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEiKREAEEEE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 372 IEEMKEKEKRKKLEEQRergrqLMEKQRKEKELQKKQNIAREMKEMQRKQKENeerlwEIVRQTEARQQKEKDEHLRLQQ 451
Cdd:pfam02463 358 EEELEKLQEKLEQLEEE-----LLAKKKLESERLSSAAKLKEEELELKSEEEK-----EAQLLLELARQLEDLLKEEKKE 427
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1530640611 452 LAREFEERKRKEEEALLKTQQEEEDRKEEALLKIQQEEEDrkEQAKNEAERIRQEGERRQSEEMMRIEAANRIRAMGS 529
Cdd:pfam02463 428 ELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELEL--KKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKES 503
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
233-523 |
7.40e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.30 E-value: 7.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 233 LKHTNEIEKQFELERV----RLEKQRREQQIEREFEERQLKEKERIERQRNVVKEIEREAEERRRREREWLEKQRKKALH 308
Cdd:PTZ00121 1187 VRKAEELRKAEDARKAeaarKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFA 1266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 309 LQEMQAKARE-----EFERRQQLAAQLVQQQREEREKLEKQQEQARLALEKKRREEEELQKRQQAErqieemkekEKRKK 383
Cdd:PTZ00121 1267 RRQAAIKAEEarkadELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKAD---------AAKKK 1337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 384 LEEQR---ERGRQLMEKQRKEKELQKKQNIAREMKEMQRKQKENE-ERLWEIVRQTEARQQKEKDEHLRLQQLAREFEER 459
Cdd:PTZ00121 1338 AEEAKkaaEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAaKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAK 1417
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1530640611 460 KRKEEealLKTQQEEEDRKEEAllKIQQEEEDRKEQAKNEAERIRQ-EGERRQSEEMMRIEAANR 523
Cdd:PTZ00121 1418 KKADE---AKKKAEEKKKADEA--KKKAEEAKKADEAKKKAEEAKKaEEAKKKAEEAKKADEAKK 1477
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
212-450 |
8.27e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.92 E-value: 8.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 212 KSFQGEVMQEKNSYVGDQSDILKHTNEIEKQFELERVRLEKQRREQQIEREFEERQLKEKERIERQRNVVKEIEREAEER 291
Cdd:PTZ00121 1565 KAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAE 1644
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 292 RRREREWLEKQRKKALHLQEMQAKAREEFERRQQLAAQLVQQQREEREKLEKQQEQARLALEKKRREEEELQKRQQAERQ 371
Cdd:PTZ00121 1645 EKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKA 1724
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 372 ieemkekekrkkleeQRERGRQLMEKQRKEKELQKKQNIAR----EMKEMQRKQKENEERLWEIVRQTEA---RQQKEKD 444
Cdd:PTZ00121 1725 ---------------EEENKIKAEEAKKEAEEDKKKAEEAKkdeeEKKKIAHLKKEEEKKAEEIRKEKEAvieEELDEED 1789
|
....*.
gi 1530640611 445 EHLRLQ 450
Cdd:PTZ00121 1790 EKRRME 1795
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
237-526 |
1.04e-07 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 54.54 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 237 NEIEKQFELERVRLEKQRREQQIEREFEERQLKEKERIERQRNVVKEIEREAEERRRREREWLEKQRKKALHLQEMQAKA 316
Cdd:pfam13868 85 REQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEK 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 317 REEFERRQQLAAqlvqqqREEReklEKQQEQARLalekkrreeeelqkRQQAERQIEEMKEKEKRKKLEEQRERGRQlmE 396
Cdd:pfam13868 165 AEREEEREAERE------EIEE---EKEREIARL--------------RAQQEKAQDEKAERDELRAKLYQEEQERK--E 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 397 KQRKEKELQKKQNIAREMKEMQRKQKENEERlweivrqtEARQQKEKDEHLRLQQLAREFEERKRKEEEALLKTQQEEED 476
Cdd:pfam13868 220 RQKEREEAEKKARQRQELQQAREEQIELKER--------RLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEH 291
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1530640611 477 RKEeallkIQQEEEDRKEQAKNEAERIRQEGERRQSEEMMRIEAANRIRA 526
Cdd:pfam13868 292 RRE-----LEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQ 336
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
238-523 |
1.19e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.53 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 238 EIEKQFELERvRLEKQRREQQIEREFEERQLKEKERIERQRNVVKEiereaeERRRREREWLEKQRKKALHLQEMQAKAR 317
Cdd:PTZ00121 1167 EEARKAEDAK-KAEAARKAEEVRKAEELRKAEDARKAEAARKAEEE------RKAEEARKAEDAKKAEAVKKAEEAKKDA 1239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 318 EEFERRQQLAAQLVQQQREEREKLEKQQEQARLALEKKrreeEELQKRQQAERQieEMKEKEKRKKLEEQRERGRQLMEK 397
Cdd:PTZ00121 1240 EEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEA----RKADELKKAEEK--KKADEAKKAEEKKKADEAKKKAEE 1313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 398 QRKEKELQKKQNIAREMKEMQRKQKENEERLWEiVRQTEARQQKEKDEHLRLQQLAREFEERKRKEEEALLKTQQEEEDR 477
Cdd:PTZ00121 1314 AKKADEAKKKAEEAKKKADAAKKKAEEAKKAAE-AAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKK 1392
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1530640611 478 KEEALLKIQQEEEDRKEQAKNEAERIRQEGERRQSEEMMRIEAANR 523
Cdd:PTZ00121 1393 ADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKK 1438
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
255-526 |
1.40e-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: 54.98 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 255 REQQIEREFEERQLKEKERIERQRNVVKEIEREAEErrrrerewLEKQRKKALHLQEMQAKAREEFERRQQLAAQLVQQQ 334
Cdd:pfam02463 166 RLKRKKKEALKKLIEETENLAELIIDLEELKLQELK--------LKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 335 REEREKLEKQQEQARLAlekkrreeeELQKRQQAERQIEEMKEKEKRKKLEEQRERGRQLMEKQRKEKELQKKQNIAREM 414
Cdd:pfam02463 238 RIDLLQELLRDEQEEIE---------SSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERR 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 415 KEMQRKQKENEErlwEIVRQTEARQQKEKDEHLRLQQLarefeerkrkeeEALLKTQQEEEDRKEEALLKIQQEEEDRKE 494
Cdd:pfam02463 309 KVDDEEKLKESE---KEKKKAEKELKKEKEEIEELEKE------------LKELEIKREAEEEEEEELEKLQEKLEQLEE 373
|
250 260 270
....*....|....*....|....*....|....*.
gi 1530640611 495 Q----AKNEAERIRQEGERRQSEEMMRIEAANRIRA 526
Cdd:pfam02463 374 EllakKKLESERLSSAAKLKEEELELKSEEEKEAQL 409
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
234-525 |
1.62e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.15 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 234 KHTNEIEKQFELERVRLEKQRREQQIEREFEERQLKEKERIERQRNVVKEIEREAEERRRREREwLEKQRKKALHLQEMQ 313
Cdd:PTZ00121 1336 KKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKK-AEEDKKKADELKKAA 1414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 314 A--KAREEF-----ERRQQLAAQLVQQQREEREKLEKQQEQARLALEKKRREEEELQK---RQQAERQIEEMKEKEKRKK 383
Cdd:PTZ00121 1415 AakKKADEAkkkaeEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKAdeaKKKAEEAKKADEAKKKAEE 1494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 384 LEEQRERGRQLMEKQRKEKELQKKQNI--AREMKEMQRKQKENEERLWEIVRQTEarqQKEKDEHLRLQQLAREFEERKR 461
Cdd:PTZ00121 1495 AKKKADEAKKAAEAKKKADEAKKAEEAkkADEAKKAEEAKKADEAKKAEEKKKAD---ELKKAEELKKAEEKKKAEEAKK 1571
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1530640611 462 KEEEALLKTQQEEEDRKEE------------ALLKIQQEEEDRKEQAKNEAERIRQEGERRQSEEMMRIEAANRIR 525
Cdd:PTZ00121 1572 AEEDKNMALRKAEEAKKAEearieevmklyeEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKK 1647
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
256-526 |
2.06e-07 |
|
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: 54.69 E-value: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 256 EQQIEREFEErqLKE-KERIERQRNVVKEIEREAEErrrrerewLEKQRKKALHLQEMQAKARE----EFERRQQLAAQL 330
Cdd:TIGR02169 169 DRKKEKALEE--LEEvEENIERLDLIIDEKRQQLER--------LRREREKAERYQALLKEKREyegyELLKEKEALERQ 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 331 VQQQREEREKLEKQQEQ-ARLALEKKRREEEELQKRQQAERQIEEMKEKEKRKKLEEQRERGRQLMEKQRKEKELQkkqn 409
Cdd:TIGR02169 239 KEAIERQLASLEEELEKlTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKE---- 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 410 iaREMKEMQRKQKENEERLWEIvrQTEARQQKEKDEHLRLQQLAREFEERKRKEEEALLKTQQEEEDRKEEALLKIQQEE 489
Cdd:TIGR02169 315 --RELEDAEERLAKLEAEIDKL--LAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDY 390
|
250 260 270
....*....|....*....|....*....|....*..
gi 1530640611 490 EDRKEQAKNEAERIRQEGERRQSEEMMRIEAANRIRA 526
Cdd:TIGR02169 391 REKLEKLKREINELKRELDRLQEELQRLSEELADLNA 427
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
229-509 |
3.69e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.99 E-value: 3.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 229 QSDILKHTNEIEKQFELERVrlEKQRREQQiEREFEERQLKEKERIERQR-NVVKEIEREAEERRRREREWLEKQRKKAL 307
Cdd:PTZ00121 1547 KADELKKAEELKKAEEKKKA--EEAKKAEE-DKNMALRKAEEAKKAEEARiEEVMKLYEEEKKMKAEEAKKAEEAKIKAE 1623
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 308 HLQ--EMQAKAREEFERRQQLAAQLVQQQREEREKLEKQQEQARLALEKKRREEEELQKRQQAERQieEMKEKEKRKKLE 385
Cdd:PTZ00121 1624 ELKkaEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKK--AAEALKKEAEEA 1701
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 386 EQRERGRQLMEKQRKEKELQKKQNIAREMKEMQRKQKENEERLweivRQTEARqqKEKDEHLRLQQLAREFEERKRKEEE 465
Cdd:PTZ00121 1702 KKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKK----KAEEAK--KDEEEKKKIAHLKKEEEKKAEEIRK 1775
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1530640611 466 ALLKTQQEEEDRKEEallKIQQEEEDRKEQAKNEAERIRQEGER 509
Cdd:PTZ00121 1776 EKEAVIEEELDEEDE---KRRMEVDKKIKDIFDNFANIIEGGKE 1816
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
212-527 |
5.54e-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: 53.14 E-value: 5.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 212 KSFQGEVMQEKNSYVGDQSDILKHTNEI-EKQFELERVRLEKQRREQQIEREFEE--RQLKEKERIERQRNVVKEIEREA 288
Cdd:TIGR02168 235 EELREELEELQEELKEAEEELEELTAELqELEEKLEELRLEVSELEEEIEELQKElyALANEISRLEQQKQILRERLANL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 289 EERRRREREWLEKQRKKALHLQEMQAKAREEFErrqqlaaqlvqQQREEREKLEKQQEQARlalekkrreeeelQKRQQA 368
Cdd:TIGR02168 315 ERQLEELEAQLEELESKLDELAEELAELEEKLE-----------ELKEELESLEAELEELE-------------AELEEL 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 369 ERQIEEMkekekrkkleeqrergRQLMEKQRKeKELQKKQNIAREMKEMQRkqkeNEERLWEIVRQTEaRQQKEKDEHLR 448
Cdd:TIGR02168 371 ESRLEEL----------------EEQLETLRS-KVAQLELQIASLNNEIER----LEARLERLEDRRE-RLQQEIEELLK 428
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1530640611 449 LQQLARefeerkrkeeealLKTQQEEEDRKEEALLKIQQEEEDRKEQAKNEAERIRQEGERRQSEEMMRIEAANRIRAM 527
Cdd:TIGR02168 429 KLEEAE-------------LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSL 494
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
389-521 |
1.57e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 50.96 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 389 ERGRQLMEK---QRKEKELQKKQniAREMKEMQRKQKENEERLWEIVRQTEARQ--QKEKDEHLRLQQLAREFEERKRKE 463
Cdd:PRK09510 63 QYNRQQQQQksaKRAEEQRKKKE--QQQAEELQQKQAAEQERLKQLEKERLAAQeqKKQAEEAAKQAALKQKQAEEAAAK 140
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1530640611 464 EEALLKTQQEEEDRKEEALLKiqQEEEDRKEQAKNEAERIRQEGERRQSEEMMRIEAA 521
Cdd:PRK09510 141 AAAAAKAKAEAEAKRAAAAAK--KAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAA 196
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
236-529 |
2.83e-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: 50.74 E-value: 2.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 236 TNEIEKQFELERVRLEKQRREQQIEREFEERQLKEKERIERQRNVVKEIEREAEERRRREREWLEKQRKKALHLQEMQAK 315
Cdd:pfam02463 689 LAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSE 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 316 AREEFERRqqlaaqlvqqqREEREKLEKQQEQARLalekkrreeeeLQKRQQAERQIEEMKEKEKRKKLEEQRERGRQLM 395
Cdd:pfam02463 769 LSLKEKEL-----------AEEREKTEKLKVEEEK-----------EEKLKAQEEELRALEEELKEEAELLEEEQLLIEQ 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 396 EKQRKEKELQKKQNIAREMKEMQRKQKENEERLWEIVRQTEARQQKEKDEHLRLQQLAREFEERkrkeeeaLLKTQQEEE 475
Cdd:pfam02463 827 EEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELES-------KEEKEKEEK 899
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1530640611 476 DRKEEALLKIQQEEEDRKEQAKNEAERIRQEGERRQSEEMMRIEAANRIRAMGS 529
Cdd:pfam02463 900 KELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEEN 953
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
313-532 |
3.55e-06 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 49.84 E-value: 3.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 313 QAKAREEFERRQQLAAQLVQQQREEREKLEKQQEQArlalekkrreeeelQKRQQAERQieemkeKEKRKKLEEQRERGR 392
Cdd:TIGR02794 45 PGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEA--------------EKQRAAEQA------RQKELEQRAAAEKAA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 393 QLMEKQRKEKELQKKQniAREMKEMQRK-QKENEERLWEIVRQTEARQQKEKDEHLRLQQLArefeerkrkEEEALLKTQ 471
Cdd:TIGR02794 105 KQAEQAAKQAEEKQKQ--AEEAKAKQAAeAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEA---------KKKAEEAKK 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1530640611 472 QEEEDRKEEALLKIQQEEEDRKEQAKNEAERIRQEGERRQSEEMMRIEAANRIRAMGSGNL 532
Cdd:TIGR02794 174 KAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAEL 234
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
363-503 |
7.64e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 49.01 E-value: 7.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 363 QKRQQAERQIeemkekekrkkleeqRERGRQLmekQRKEKEL-QKKQNIAREMKEMQRKQKENEERLWEIVRQTEARQQK 441
Cdd:PRK12704 68 KLRNEFEKEL---------------RERRNEL---QKLEKRLlQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKK 129
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1530640611 442 EKD-EHLRLQQLAREFEERKRKEEEA--LLKTQQEEEDRKEEALLkIQQEEEDRKEQAKNEAERI 503
Cdd:PRK12704 130 EEElEELIEEQLQELERISGLTAEEAkeILLEKVEEEARHEAAVL-IKEIEEEAKEEADKKAKEI 193
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
255-527 |
1.35e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 47.99 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 255 REQQIEREFEERQLKEKERIERQRNVVKEIEREAEERRRREREWLEKQRKKALHLQE---------MQAKAREEFERRQQ 325
Cdd:pfam13868 24 RDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEqieereqkrQEEYEEKLQEREQM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 326 LAAQLVQQQREEREKLEKQQEQARLALE-KKRREEEELQKRQQAERQIEEMKEKEKRKKLEEQRERGRQLMEKQRKEKEL 404
Cdd:pfam13868 104 DEIVERIQEEDQAEAEEKLEKQRQLREEiDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 405 QKKQNIAREMKEMQRKQKENEE----RLWEIVRQTEARQQKEKDEHLRLQQLAREFEERKRKEEEALLKTQQEEEDRKEE 480
Cdd:pfam13868 184 REIARLRAQQEKAQDEKAERDElrakLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEF 263
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1530640611 481 ALLKIQQEEEDRKEQAKNEAERIRQEGERRQSEEMMRIEAANRIRAM 527
Cdd:pfam13868 264 ERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAER 310
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
212-451 |
2.96e-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: 47.74 E-value: 2.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 212 KSFQGEVMQEKNSYvgdQSDILKHTNEIEkqfelervRLEKQRREQQIEREFEERQLKEKERI----ERQRNVVKEIERE 287
Cdd:TIGR02168 273 RLEVSELEEEIEEL---QKELYALANEIS--------RLEQQKQILRERLANLERQLEELEAQleelESKLDELAEELAE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 288 AEERRRREREWLEKQRKKalhLQEMQAKaREEFERRQQLAAQLVQQQREEREKLEKQQEQARLALEKKRREEEELQKRQq 367
Cdd:TIGR02168 342 LEEKLEELKEELESLEAE---LEELEAE-LEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRR- 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 368 aERQIEEMKEKEKRKKLEEQRERGRQLMEKQRKEKELQKKQNIAREMKEMQRKQKENEERLWEIVRQTEARQQKEKDEHL 447
Cdd:TIGR02168 417 -ERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLE 495
|
....
gi 1530640611 448 RLQQ 451
Cdd:TIGR02168 496 RLQE 499
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
240-423 |
4.94e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 46.48 E-value: 4.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 240 EKQFELERVRLEKQRREQQIEREFEERQLKEKERIER-----QRNVVKEIEREAEERRRREREWLEKQRKKALHLQEMQA 314
Cdd:pfam15709 340 AERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREeleleQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQE 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 315 KAR---EEFERRQQLAAQLVQQQREEREKLEKQ---QEQARLALEKKRREEEELQKRQQAERQieemkekekrkkLEEQR 388
Cdd:pfam15709 420 RARqqqEEFRRKLQELQRKKQQEEAERAEAEKQrqkELEMQLAEEQKRLMEMAEEERLEYQRQ------------KQEAE 487
|
170 180 190
....*....|....*....|....*....|....*
gi 1530640611 389 ERGRQLMEKQRKEKELQKKQNIAREMKEMQRKQKE 423
Cdd:pfam15709 488 EKARLEAEERRQKEEEAARLALEEAMKQAQEQARQ 522
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
299-513 |
5.20e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 46.48 E-value: 5.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 299 LEKQRKKALHLQEMQAKARE-EFERRQQLAAQLVQQQREEREKLEKQQEQARLALEKKRREEEELQKRQQAERQIEEMKE 377
Cdd:pfam15709 328 REQEKASRDRLRAERAEMRRlEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEE 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 378 KEKRKKLEEQRERGRQLMEK-QRKEKELQKK--QNIAREMKEMQRKQKENEERLWEIVRQTEARQQKEKDEHLRLQQLAR 454
Cdd:pfam15709 408 RKQRLQLQAAQERARQQQEEfRRKLQELQRKkqQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQRQKQEAE 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1530640611 455 EfeerkrkeeeallKTQQEEEDRKeeallkiQQEEEdrkeQAKNEAERIRQEGERRQSE 513
Cdd:pfam15709 488 E-------------KARLEAEERR-------QKEEE----AARLALEEAMKQAQEQARQ 522
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
388-533 |
5.26e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.85 E-value: 5.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 388 RERGRQLMEKQRKEKELQKKQNIAREMKEMQRKQKENEERLWEIVRQTEARQQKEKDEHLRLQQLAREFEERKRKEEEAL 467
Cdd:COG1196 636 LRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEE 715
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 468 LKTQQEEEDRKEEALLKIQQEEEDRKEQAK----NEAERIRQEGERRQSEEMMRIEAANRIRAMGSGNLL 533
Cdd:COG1196 716 RLEEELEEEALEEQLEAEREELLEELLEEEelleEEALEELPEPPDLEELERELERLEREIEALGPVNLL 785
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
239-533 |
5.94e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.60 E-value: 5.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 239 IEKQFELERVRLEKQRREQQIEREFEERQlKEKERIERQRNVVKEIereaeerrrrerewLEKQRKKALHLQEMQAKARE 318
Cdd:TIGR02169 694 QSELRRIENRLDELSQELSDASRKIGEIE-KEIEQLEQEEEKLKER--------------LEELEEDLSSLEQEIENVKS 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 319 EFERrqqlaaqlvQQQREEREKLEKQQEQARLALEKKRREEEELQKRQQAERQIEEMKEKEKRKKLEEQRERGRQLMEKQ 398
Cdd:TIGR02169 759 ELKE---------LEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKE 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 399 RKEKELQKKQNIAREMKEmqrKQKENEERLWEIVRQTEARQQKEKDEHLRLQQLAREFEERKRKEEEaLLKTQQEEEDRK 478
Cdd:TIGR02169 830 YLEKEIQELQEQRIDLKE---QIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDE-LEAQLRELERKI 905
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1530640611 479 EEALLKIQQEEE---DRKEQAKNEAERIRQEGERRQSEE-------------MMRIEAANRIRAMGSGNLL 533
Cdd:TIGR02169 906 EELEAQIEKKRKrlsELKAKLEALEEELSEIEDPKGEDEeipeeelsledvqAELQRVEEEIRALEPVNML 976
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
395-525 |
9.24e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 9.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 395 MEKQRKEKELQKKQniarEMKEMQRK-QKENEERLWEIVRQTEARQQKEkdEHLRLQQLAREFEERKRKEEEALLKTQQE 473
Cdd:PRK12704 51 AEAIKKEALLEAKE----EIHKLRNEfEKELRERRNELQKLEKRLLQKE--ENLDRKLELLEKREEELEKKEKELEQKQQ 124
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1530640611 474 EEDRKEEALLKIQQEEEDR--------KEQAKNEA-ERIRQEgerrqseemMRIEAANRIR 525
Cdd:PRK12704 125 ELEKKEEELEELIEEQLQElerisgltAEEAKEILlEKVEEE---------ARHEAAVLIK 176
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
396-528 |
9.42e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 45.63 E-value: 9.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 396 EKQRKEKELQKKQNIarEMKEMQRKQKENEERLWEIVRQTEaRQQKEKDEHLRLQQlarefeerkrkeEEALLKTQQEEE 475
Cdd:COG2268 220 NREAEEAELEQEREI--ETARIAEAEAELAKKKAEERREAE-TARAEAEAAYEIAE------------ANAEREVQRQLE 284
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1530640611 476 DRKEEALLKIQQEEEDRKEQAKNEAERIRQEGERRQSEEMMRIEAAnRIRAMG 528
Cdd:COG2268 285 IAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAEAE-AIRAKG 336
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
244-544 |
1.01e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 45.63 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 244 ELERVRLEKQRREQQIEREFEERQLKEKERIERQRNVVKEIEREAEERRRREREWLEKQRKKalhlQEMQAKAREEFERR 323
Cdd:pfam02029 60 EEEAFLDRTAKREERRQKRLQEALERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKR----DSRLGRYKEEETEI 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 324 QQLAAQLVQQQREEREKLEKQQEQARLALEKKRREEEELQKRQQAERQIEEMKEKEKRKKLEEQRERGR----------Q 393
Cdd:pfam02029 136 REKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHpevksqngeeE 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 394 LMEKQRKEKELQKKQNIAREMKEMQRKQKENEERLWEIVRQteaRQQKEKDEHLRLQQlarefEERKRKEEEALLKTQQE 473
Cdd:pfam02029 216 VTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQKLEELRRR---RQEKESEEFEKLRQ-----KQQEAELELEELKKKRE 287
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1530640611 474 EEDrkeeallKIQQEEEDRKEQAkneaeriRQEGERRQSEEMMRIEAANRIRAMGSGNLLPAMSSRGSSGD 544
Cdd:pfam02029 288 ERR-------KLLEEEEQRRKQE-------EAERKLREEEEKRRMKEEIERRRAEAAEKRQKLPEDSSSEG 344
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
336-501 |
1.43e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 44.80 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 336 EEREKLEKQQEQarlalekkrreeeELQKRQQAERQieemkekekrkkLEEQRERGRQLMEKQRKEKELQKKQniaremk 415
Cdd:PRK09510 79 EQRKKKEQQQAE-------------ELQQKQAAEQE------------RLKQLEKERLAAQEQKKQAEEAAKQ------- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 416 eMQRKQKENEErlwEIVRQTEARQQKEKDEHLRLQQLAREFEERKRKEEEALLKTQQEEEDRKEEALLKIQQEEEDRKEQ 495
Cdd:PRK09510 127 -AALKQKQAEE---AAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKK 202
|
....*.
gi 1530640611 496 AKNEAE 501
Cdd:PRK09510 203 AEAEAK 208
|
|
| ChtBD2 |
smart00494 |
Chitin-binding domain type 2; |
633-678 |
1.52e-04 |
|
Chitin-binding domain type 2;
Pssm-ID: 214696 [Multi-domain] Cd Length: 49 Bit Score: 39.73 E-value: 1.52e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1530640611 633 GDCNFSYDQDLlcPHPSDSSRYLQCTPmigrrGRWTERNCPPTLVF 678
Cdd:smart00494 1 NECPGRGDGLY--PHPTDCSKYYQCSN-----GRPIVGSCPAGLVF 39
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
244-514 |
2.26e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 244 ELERVRLEKQRREQQIERE---FEERQLKEKERIERQRNVVKEIEREAEERRRREREWLEKQRKKALHLQEMQAKAREEF 320
Cdd:PTZ00121 1078 DFDFDAKEDNRADEATEEAfgkAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIA 1157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 321 ERRQQLAAQLVQQQREEREKLEKQQEQARLALEKKRREEEELQKRQQAERQIEEMKEKEKRKKLEEQRERGRQLMEKQRK 400
Cdd:PTZ00121 1158 RKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKK 1237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 401 EKELQKKqniAREMKEMQRKQKENEERLWEIVRQTEARQQKEKDEHLRLQQLAREFEERKRKEEEALLKTQQ----EEED 476
Cdd:PTZ00121 1238 DAEEAKK---AEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEakkkAEEA 1314
|
250 260 270
....*....|....*....|....*....|....*...
gi 1530640611 477 RKEEALLKIQQEEEDRKEQAKNEAERIRQEGERRQSEE 514
Cdd:PTZ00121 1315 KKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEA 1352
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
240-521 |
3.71e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.77 E-value: 3.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 240 EKQFELERVRLEKQRREQQIEREFEERQLKEKERIERQRNVVKEIEREAEErrrrerewLEKQRKKALHLQEMQAKAREE 319
Cdd:COG1196 344 EELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA--------AAELAAQLEELEEAEEALLER 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 320 FERRQQLAAQLVQQQREEREKLE----KQQEQARLALEKKRREEEELQKRQQAERQIEEMKEKEKRKKLEEQRERGRQLM 395
Cdd:COG1196 416 LERLEEELEELEEALAELEEEEEeeeeALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 396 EKQRKEKELQKKQNIARemkemqRKQKENEERLWEIVRqtEARQQKEKDEHLRLQQLAREFEERKRKEEEALLKTQQEEE 475
Cdd:COG1196 496 LLEAEADYEGFLEGVKA------ALLLAGLRGLAGAVA--VLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLK 567
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1530640611 476 DRKEEALLKIQQEEEDRKEQAKNEAERIRQEGERRQSEEMMRIEAA 521
Cdd:COG1196 568 AAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADA 613
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
238-527 |
3.91e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.81 E-value: 3.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 238 EIEKQFELERVRLEKQRREQQIEREFEERQLKEKERIERQRNVVKEIEREAEERRRREREWLEKQRKKALHLQEMQAKAR 317
Cdd:pfam02463 751 EEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKI 830
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 318 EEFERRQQLAAQLVQQQREEREKLEKQQEQARLALEKKRREEEELQKRQQAERQIEEMKEKEKRKKLEEQRERGRQLMEK 397
Cdd:pfam02463 831 KEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLN 910
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 398 QRKEKELQKKQNIAREMKEMQRKQKENEERLWEIVRQTEARQQKEKDEHLRLQQLarefeerkrkeeeallkTQQEEEDR 477
Cdd:pfam02463 911 LLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRL-----------------LLAKEELG 973
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1530640611 478 KEEALLKIQQEEEDRKEQAKNEAERIRQEGERRQSEEMMRIEAANRIRAM 527
Cdd:pfam02463 974 KVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFL 1023
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
216-525 |
3.94e-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: 43.89 E-value: 3.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 216 GEVMQEKNSYVGDQSDILKHTNEIEKQFELERvRLEKQR---REQQIEREFEERQL-KEKERIERQRNVVKEIEREAEER 291
Cdd:TIGR02168 663 GGSAKTNSSILERRREIEELEEKIEELEEKIA-ELEKALaelRKELEELEEELEQLrKELEELSRQISALRKDLARLEAE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 292 RRRerewLEKQRKKALHLQEMQAKAREEFERRQQLAAQLVQQQREEREKLEKQQEQARLALEKKRREEEELQKRQQAERQ 371
Cdd:TIGR02168 742 VEQ----LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNE 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 372 IEEMKEKEKRKKLEEQRERGRQLME-KQRKEKELQKKQNIAREMKEMQRKQKENEERL---WEIVRQTEARQQKEKDEHL 447
Cdd:TIGR02168 818 EAANLRERLESLERRIAATERRLEDlEEQIEELSEDIESLAAEIEELEELIEELESELealLNERASLEEALALLRSELE 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 448 RLQQLAREFEERKRKEEEALLKTQQEEED---RKEEALLKIQQEEEDRKEQAKNEAERIRQEGERRQSEEMmriEAANRI 524
Cdd:TIGR02168 898 ELSEELRELESKRSELRRELEELREKLAQlelRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEE---EARRRL 974
|
.
gi 1530640611 525 R 525
Cdd:TIGR02168 975 K 975
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
339-527 |
4.08e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 4.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 339 EKLEKQQEQARLALEKKRREEEELQKRQQAERQIEEMKEKEkrkklEEQRERGRQLMEKQRKEKELQKKQNIAREMKEMQ 418
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAEL-----EELREELEKLEKLLQLLPLYQELEALEAELAELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 419 RKQKENEERLWEIVRQTEARQQKEKDEHLRLQQLAREFEERKRKEEEALLKTQQEEEDRKEEallkiQQEEEDRKEQAKN 498
Cdd:COG4717 146 ERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQR-----LAELEEELEEAQE 220
|
170 180
....*....|....*....|....*....
gi 1530640611 499 EAERIRQEGERRQsEEMMRIEAANRIRAM 527
Cdd:COG4717 221 ELEELEEELEQLE-NELEAAALEERLKEA 248
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
238-351 |
8.47e-04 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 40.41 E-value: 8.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 238 EIEKQFELERVRLEKQRREQQIEREFEERQLKEKE--RIERQRNVVKEIEREAEERRRREREWLEKQRKKALHLQ--EMQ 313
Cdd:pfam05672 28 EREEQERLEKEEEERLRKEELRRRAEEERARREEEarRLEEERRREEEERQRKAEEEAEEREQREQEEQERLQKQkeEAE 107
|
90 100 110
....*....|....*....|....*....|....*...
gi 1530640611 314 AKAREEFERRqqlaaqlvqqqREEREKLEKQQEQARLA 351
Cdd:pfam05672 108 AKAREEAERQ-----------RQEREKIMQQEEQERLE 134
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
396-496 |
1.09e-03 |
|
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.
Pssm-ID: 464032 [Multi-domain] Cd Length: 221 Bit Score: 41.23 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 396 EKQRKEKELQKKQNIAREMKEMQRKQKENEERLWEIVRQtEARQQKEKDEHLRLQQLAREFEERKRKEEEALL------- 468
Cdd:pfam13904 65 QRQRQKELQAQKEEREKEEQEAELRKRLAKEKYQEWLQR-KARQQTKKREESHKQKAAESASKSLAKPERKVSqeeakev 143
|
90 100 110
....*....|....*....|....*....|....*..
gi 1530640611 469 -------KTQQEEEDRKEE--ALLKIQQEEEDRKEQA 496
Cdd:pfam13904 144 lqewerkKLEQQQRKREEEqrEQLKKEEEEQERKQLA 180
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
385-524 |
1.37e-03 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 39.64 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 385 EEQRERgrqlMEKQRKEKELQKKQniarEMKEMQRKQKENEERLWEIVRQTEARQQKEKDEHLRLQQlarefeerkrkee 464
Cdd:pfam05672 24 REQRER----EEQERLEKEEEERL----RKEELRRRAEEERARREEEARRLEEERRREEEERQRKAE------------- 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1530640611 465 eallKTQQEEEDRKEEALLKIQQEEEDRKEQAKNEAERIRQEGERR-QSEEMMRIEAANRI 524
Cdd:pfam05672 83 ----EEAEEREQREQEEQERLQKQKEEAEAKAREEAERQRQEREKImQQEEQERLERKKRI 139
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
303-521 |
2.09e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 41.01 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 303 RKKALHLQEMQAKAREEFERrqqlaaqlvqqqrEEREKLEKQQEQARLAlekkrreeeelQKRQQAERQIeemkekekrk 382
Cdd:COG2268 191 RRKIAEIIRDARIAEAEAER-------------ETEIAIAQANREAEEA-----------ELEQEREIET---------- 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 383 kleeqRERGRQLMEKQRKEKELQKKQNIAREMKEMQ-RKQKENEERlwEIVRQTE-ARQQKEkdehLRLQQLArefeerk 460
Cdd:COG2268 237 -----ARIAEAEAELAKKKAEERREAETARAEAEAAyEIAEANAER--EVQRQLEiAERERE----IELQEKE------- 298
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1530640611 461 rkeeeALLKTQQEEEDRKEEALLKIQQEEedrkEQAKNEAERIRQEGErRQSEEMMRIEAA 521
Cdd:COG2268 299 -----AEREEAELEADVRKPAEAEKQAAE----AEAEAEAEAIRAKGL-AEAEGKRALAEA 349
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
241-508 |
2.18e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.58 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 241 KQFELERVRLEKQRREQQIEREFEERQLKEKE-RIERQRnvvKEIEREAEERRRREREWLE-KQRKKALHLQEMQAKARE 318
Cdd:TIGR02168 235 EELREELEELQEELKEAEEELEELTAELQELEeKLEELR---LEVSELEEEIEELQKELYAlANEISRLEQQKQILRERL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 319 EFERRQQLAAQlvqqqrEEREKLEKQQEQARLALEKKRREEEELQKRQQAERQIEEMKEKEKRKKLEEQRERGRQLMEKQ 398
Cdd:TIGR02168 312 ANLERQLEELE------AQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLR 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 399 RKEKELQKKQNIAREMKEMQRKQKE----NEERLWEIVRQTEARQQKEKDEHLRlQQLAREFEERKRKEEEALLKTQQEE 474
Cdd:TIGR02168 386 SKVAQLELQIASLNNEIERLEARLErledRRERLQQEIEELLKKLEEAELKELQ-AELEELEEELEELQEELERLEEALE 464
|
250 260 270
....*....|....*....|....*....|....*...
gi 1530640611 475 EDRKEEALLK-IQQEEEDRKEQAKNEA---ERIRQEGE 508
Cdd:TIGR02168 465 ELREELEEAEqALDAAERELAQLQARLdslERLQENLE 502
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
389-600 |
3.97e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.20 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 389 ERGRQLMEKQRKEKEL--QKKQNIAREMKEMQRKQKENEERLWEIVRQTEARQQK----EKDEHLRLQQLAREFEERKRK 462
Cdd:COG3883 129 DADADLLEELKADKAEleAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALlaqlSAEEAAAEAQLAELEAELAAA 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 463 EEEALLKTQQEEEDRKEEALLKIQQEEEDRKEQAKNEAERIRQEGERRQSEEMMRIEAANRIRAMGSGNLLPAMSSRGSS 542
Cdd:COG3883 209 EAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGG 288
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1530640611 543 GDNGHAHTFHPEATDFPGRVDFQTSQTLPVDPNVIHFTAAPSTVPSAVPAWVRGPQPW 600
Cdd:COG3883 289 AGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAVVGGASAGGGGGSGGGGGSSGGGSG 346
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
386-527 |
5.20e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 39.93 E-value: 5.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 386 EQRERGRQLMEKQRKeKELQKKQniaREMKEMQRKQKENEERLWEIVRQTEARQQKEKDE-HLRLQQLAREFEERKRKEE 464
Cdd:pfam15709 333 ASRDRLRAERAEMRR-LEVERKR---REQEEQRRLQQEQLERAEKMREELELEQQRRFEEiRLRKQRLEEERQRQEEEER 408
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1530640611 465 EALLKTQ--QEEEDRKEEALLKIQQEEEDRKEQakNEAERIRQEGERRQSEEMMRIEAANRIRAM 527
Cdd:pfam15709 409 KQRLQLQaaQERARQQQEEFRRKLQELQRKKQQ--EEAERAEAEKQRQKELEMQLAEEQKRLMEM 471
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
345-514 |
5.40e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 40.08 E-value: 5.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 345 QEQARLALEKKRREEEELQKRQQAERQIEEMKEKEKRKKLEEQRERGRQLMEKQRKEKE--LQKKQNIAREMKEMQRKQK 422
Cdd:PRK12705 26 KKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEErlVQKEEQLDARAEKLDNLEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 423 ENEERLWEIVRQTEARQQKEKDEHLRLQQLAREFEERKRKEEEALLktqqeEEDRKEEALLKIQQEEEDRKEQAKNEAER 502
Cdd:PRK12705 106 QLEEREKALSARELELEELEKQLDNELYRVAGLTPEQARKLLLKLL-----DAELEEEKAQRVKKIEEEADLEAERKAQN 180
|
170
....*....|..
gi 1530640611 503 IRQEGERRQSEE 514
Cdd:PRK12705 181 ILAQAMQRIASE 192
|
|
| CBM_14 |
pfam01607 |
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ... |
646-693 |
6.01e-03 |
|
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is found in chitin binding proteins particularly peritrophic matrix proteins of insects and animal chitinases. Copies of the domain are also found in some baculoviruses. Relevant references that describe proteins with this domain include. It is an extracellular domain that contains six conserved cysteines that probably form three disulphide bridges. Chitin binding has been demonstrated for a protein containing only two of these domains.
Pssm-ID: 426342 [Multi-domain] Cd Length: 53 Bit Score: 35.47 E-value: 6.01e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1530640611 646 PHPSDSSRYLQCTpmigrRGRWTERNCPPTLVFLHAHAACG-AQNVSSC 693
Cdd:pfam01607 10 ADPGDCSKYYVCS-----NGEAVEFTCPNGLVFDPTLGICDyPDNVVDC 53
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
338-527 |
6.17e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 6.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 338 REKLEKQQEQARLALEKKRRE-EEELQKRQQAERQIEEMKEKEKRKKLEEQRERGRQLMEKQRK-EKELQKKQNIAREMK 415
Cdd:COG4717 295 REKASLGKEAEELQALPALEElEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEElEEELQLEELEQEIAA 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 416 EMQRKQKENEERLWEIVRQTEARQQKEKDEHLRLQQLAREFEERKRKEEEALLKTQQEEEDRKEEALLKIQQEEED-RKE 494
Cdd:COG4717 375 LLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEElREE 454
|
170 180 190
....*....|....*....|....*....|....
gi 1530640611 495 QAKNEAERIRQEGERRQSEEMMRIE-AANRIRAM 527
Cdd:COG4717 455 LAELEAELEQLEEDGELAELLQELEeLKAELREL 488
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
234-506 |
8.12e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.66 E-value: 8.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 234 KHTNEI-EKQFELERVRLEKQRREQQIeREFEERQLKEKERIERQRNVVKEIEReaeerrrrerewLEKQRKKALHLQEM 312
Cdd:PRK03918 235 ELKEEIeELEKELESLEGSKRKLEEKI-RELEERIEELKKEIEELEEKVKELKE------------LKEKAEEYIKLSEF 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 313 qakaREEFERRQQLAAQLVQQQREEREKLEKQQEQArlaLEKKRREEEELQKRQQAERQIEEMKEKEKRKkleeqrERGR 392
Cdd:PRK03918 302 ----YEEYLDELREIEKRLSRLEEEINGIEERIKEL---EEKEERLEELKKKLKELEKRLEELEERHELY------EEAK 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 393 QL---MEKQRKEKELQKKQNIAREMKEMQRKQKENEERLWEIVRQTEARQQKEKDEHLRLQQLarefeeRKRKEEEALLK 469
Cdd:PRK03918 369 AKkeeLERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEEL------KKAKGKCPVCG 442
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1530640611 470 TQQEEEDRKE---------EALLKIQQEEEDRKEQAKNEAERIRQE 506
Cdd:PRK03918 443 RELTEEHRKElleeytaelKRIEKELKEIEEKERKLRKELRELEKV 488
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
217-515 |
9.64e-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: 39.28 E-value: 9.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 217 EVMQEKNSYVGDQSDILKHTNEIEK-----QFELERVRLEKQRREQ-------QIEREFEERQLKEKER-------IERQ 277
Cdd:TIGR02169 227 ELLKEKEALERQKEAIERQLASLEEeleklTEEISELEKRLEEIEQlleelnkKIKDLGEEEQLRVKEKigeleaeIASL 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 278 RNVVKEIEREAEERRRREREWLEKQRKKALHLQEMQAKAREEFERRQQLAAQLVQQQREEREKLEKQQEQARLALEKKRR 357
Cdd:TIGR02169 307 ERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDE 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1530640611 358 EEEELQKRQQAERQIEEMKEKEKRKKLEEQRERGRQLMEKQRKEKELQKKQNIAREMKEMQRKQKENEERLweivRQTEA 437
Cdd:TIGR02169 387 LKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKL----EQLAA 462
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1530640611 438 RQQKEKDEHLRLQQlarefeerkrkeeeallkTQQEEEDRKEEAllkiqQEEEDRKEqAKNEAERIRQEGERRQSEEM 515
Cdd:TIGR02169 463 DLSKYEQELYDLKE------------------EYDRVEKELSKL-----QRELAEAE-AQARASEERVRGGRAVEEVL 516
|
|
| |
