|
Name |
Accession |
Description |
Interval |
E-value |
| SCAPER_N |
pfam16501 |
S phase cyclin A-associated protein in the endoplasmic reticulum; SCAPER_N is a short highly ... |
107-204 |
5.62e-57 |
|
S phase cyclin A-associated protein in the endoplasmic reticulum; SCAPER_N is a short highly conserved region close to the N-terminus. SCAPER is localized to the endoplasmic reticulum and is a substrate for cyclin A/Cdk2. It associates with cyclin A and localizes to the ER. One theory suggests that SCAPER functions to create a local high concentration of cyclin A2 in the cytoplasm. Alternatively, SCAPER might be acting to sequester a portion of cellular cyclin A2 that could then be readily available for nuclear translocation, which may be needed for exit from G0 phase.
Pssm-ID: 406813 Cd Length: 98 Bit Score: 191.85 E-value: 5.62e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 107 KTRQPRKVDLRARYWAFLFDNLRRAVDEIYVTCESDQSVVECREVLMMLDNYVRDFKALIDWIQLQEKLEKTDAQNRPTS 186
Cdd:pfam16501 1 STGRDKKSELRARYWAFLFDNLQRAVDEIYQTCESDESVVECKEVIMVLDNYTRDFKALIEWFRLKWDYENTPPPQRPTS 80
|
90
....*....|....*...
gi 176866331 187 LAWEVRKMSPGRHVMSSP 204
Cdd:pfam16501 81 LAWEVRKSSPGKSVNKSP 98
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
331-690 |
1.69e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 72.48 E-value: 1.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 331 KEMEKTPVIEPQSMAEVLAKKEEMADRLEKANEEAIASAIAEEEQLTREIQAENSELETDNESDFSASIGSGSCGLNLDW 410
Cdd:PTZ00121 1413 AAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKA 1492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 411 SEML--ADyEAREPWRQSTSWGDIVEEEPARPPGHGIHMHEKLSSPSRKRtiAESKKKHEEKQlKAQQLRDKLREEKTHK 488
Cdd:PTZ00121 1493 EEAKkkAD-EAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKK--AEEKKKADELK-KAEELKKAEEKKKAEE 1568
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 489 LQKLMEREKDVRKWKEELLDQRRKMMEEKLLHAEFKRELQLQAIvKKAQEEEAKVNEIafiNTLEAQNKRHDVLAKLDEY 568
Cdd:PTZ00121 1569 AKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEA-KKAEEAKIKAEEL---KKAEEEKKKVEQLKKKEAE 1644
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 569 EQRLNELQEERQRRQEEKQARD--EAVQERKRVLE---AERQARVEELLMKRREQEARIEQQRQEKDRAREDAARERARD 643
Cdd:PTZ00121 1645 EKKKAEELKKAEEENKIKAAEEakKAEEDKKKAEEakkAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKA 1724
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 176866331 644 REERLAALSAAQQEAMEELQKKIQMKHDESSRRHMEQMEQRKEKAAE 690
Cdd:PTZ00121 1725 EEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAE 1771
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
349-624 |
2.18e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 65.45 E-value: 2.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 349 AKKEEMADRLEK---ANEEAIASAIAEEEQLTREIQA-----ENSELETDNESDFSASIGSGSCGLNLDWSEMLADYEAR 420
Cdd:PRK02224 359 EELREEAAELESeleEAREAVEDRREEIEELEEEIEElrerfGDAPVDLGNAEDFLEELREERDELREREAELEATLRTA 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 421 EpwrqstswGDIVEEEPARPPGHGIHMHEKLSSPSRKRTIAESKKKHEEKQLKAQQLRDKL--REEKTHKLQKLMEREKD 498
Cdd:PRK02224 439 R--------ERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVeeVEERLERAEDLVEAEDR 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 499 V------RKWKEELLDQRRKMMEEKLLHAEFKR----ELQLQAIVKKAQEEEAKVN------EIAFIN--------TLEA 554
Cdd:PRK02224 511 IerleerREDLEELIAERRETIEEKRERAEELReraaELEAEAEEKREAAAEAEEEaeeareEVAELNsklaelkeRIES 590
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 176866331 555 QNKRHDVLAKLDEYEQRLNELQEERQRRQEEKQARDEAVQ---ERKRVLEAERQ-ARVEELLMKRREQEARIEQ 624
Cdd:PRK02224 591 LERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAekrERKRELEAEFDeARIEEAREDKERAEEYLEQ 664
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
265-832 |
2.28e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.55 E-value: 2.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 265 AKKDAEGWETVQRGRSMRPRAKVSPV-LVHASPKDDSDKENQHVQPSPQDKSQDVREQEppipqEPSKEMEKTPVIEPQS 343
Cdd:PTZ00121 1235 AKKDAEEAKKAEEERNNEEIRKFEEArMAHFARRQAAIKAEEARKADELKKAEEKKKAD-----EAKKAEEKKKADEAKK 1309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 344 MAEVLAKKEEMADRLEKANEEA-IASAIAEE-----EQLTREIQAENSELETDNESDFSASIGSGSCGLNLDWSEMLAD- 416
Cdd:PTZ00121 1310 KAEEAKKADEAKKKAEEAKKKAdAAKKKAEEakkaaEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEe 1389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 417 -YEAREPWRQSTSWGDIVEE-----------EPARPPGHGIHMHEKLSSPSRKRTIAESKKKHEEKQLKAQQLRDKLRE- 483
Cdd:PTZ00121 1390 kKKADEAKKKAEEDKKKADElkkaaaakkkaDEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEa 1469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 484 EKTHKLQKLMEREK---DVRKWKEEL---LDQRRKMMEEK-----LLHAEFKR---ELQLQAIVKKAQE-----EEAKVN 544
Cdd:PTZ00121 1470 KKADEAKKKAEEAKkadEAKKKAEEAkkkADEAKKAAEAKkkadeAKKAEEAKkadEAKKAEEAKKADEakkaeEKKKAD 1549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 545 EIAFINTLEAQNKRHDVLAKLDEYEQRLNELqeerQRRQEEKQARDEAVQERKRVLEAERQARVEELlmkRREQEARIEQ 624
Cdd:PTZ00121 1550 ELKKAEELKKAEEKKKAEEAKKAEEDKNMAL----RKAEEAKKAEEARIEEVMKLYEEEKKMKAEEA---KKAEEAKIKA 1622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 625 QRQEKDRAREDAARERARDREERLAALSAAQQEAMEELQKKIQMKHDEssrrhmeqmEQRKEKAAELssgRHANTDYAPK 704
Cdd:PTZ00121 1623 EELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKA---------EEDKKKAEEA---KKAEEDEKKA 1690
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 705 LTPYERKKQcslcnvvitsEVHLFSHIKGKRHQQAVRDSSSIQGRELSDEEVEHLSQKKYivdivTDSIVSSDNAKDGEE 784
Cdd:PTZ00121 1691 AEALKKEAE----------EAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAE-----EDKKKAEEAKKDEEE 1755
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 176866331 785 RQKARKKAKKLRARMNSRAKEYETCMEAKSQTSDSPYKAKLQRLVKDL 832
Cdd:PTZ00121 1756 KKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDI 1803
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
348-663 |
5.04e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.19 E-value: 5.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 348 LAKKEEMADRLEKANEEaIASAIAEEEQLTREIQAENSELETdNESDFSAsigsgscgLNLDWSEMLADYEAREpwrqst 427
Cdd:COG1196 231 LLKLRELEAELEELEAE-LEELEAELEELEAELAELEAELEE-LRLELEE--------LELELEEAQAEEYELL------ 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 428 swGDIVEEEparppghGIHMHEKLSSPSRKRTIAESKKKHEEKQLKAQQLRDKLREEKthklQKLMEREKDVRKWKEELL 507
Cdd:COG1196 295 --AELARLE-------QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELE----EELEEAEEELEEAEAELA 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 508 DQrrkmmEEKLLHAEFKRELQLQAIVKKAQEEEAKVNEIAfintlEAQNKRHDVLAKLDEYEQRLNELqeeRQRRQEEKQ 587
Cdd:COG1196 362 EA-----EEALLEAEAELAEAEEELEELAEELLEALRAAA-----ELAAQLEELEEAEEALLERLERL---EEELEELEE 428
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 176866331 588 ARDEAVQERKRVLEAERQARVEELLMKRREQEARIEQQRQEKDRAREDAARERARDREERLAALSAAQQEAMEELQ 663
Cdd:COG1196 429 ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
304-629 |
1.34e-09 |
|
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: 62.83 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 304 NQHVQPSPQDKSQDVREQeppipQEPSKEMEKTPV-IEPQSMAEVLAKKEEMADRlEKANEEAI---ASAIAEEEQLTRE 379
Cdd:pfam17380 272 NQLLHIVQHQKAVSERQQ-----QEKFEKMEQERLrQEKEEKAREVERRRKLEEA-EKARQAEMdrqAAIYAEQERMAME 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 380 IQAENSELETDNESDFSASIGSGSCGLNLdwsEMLADYEAREPWRQSTSWGDIVEEEPARppghgihmHEKLSSPSRKRT 459
Cdd:pfam17380 346 RERELERIRQEERKRELERIRQEEIAMEI---SRMRELERLQMERQQKNERVRQELEAAR--------KVKILEEERQRK 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 460 IAESKKKHEEKQLKAQQLRD----KLREEKTHKLQKL----MEREKDVRKWKEELLDQRRKMMEeklLHAEFKRELQLQA 531
Cdd:pfam17380 415 IQQQKVEMEQIRAEQEEARQrevrRLEEERAREMERVrleeQERQQQVERLRQQEEERKRKKLE---LEKEKRDRKRAEE 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 532 IVKKAQEEEAKVNEIAFIntlEAQNKRHDVLAKLDEYEQRLNElqeerqrrqeeKQARDEAVQERKRVLEAERQARVEEL 611
Cdd:pfam17380 492 QRRKILEKELEERKQAMI---EEERKRKLLEKEMEERQKAIYE-----------EERRREAEEERRKQQEMEERRRIQEQ 557
|
330
....*....|....*...
gi 176866331 612 LMKRREQEARIEQQRQEK 629
Cdd:pfam17380 558 MRKATEERSRLEAMERER 575
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
460-713 |
3.95e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.11 E-value: 3.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 460 IAESKKKHEEKQLKAQQLRDKLREEKthklQKLMEREKDVRKWKEEL--LDQRRKMMEEKLLHAEFKRELQLQAIVKKAQ 537
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYELL----AELARLEQDIARLEERRreLEERLEELEEELAELEEELEELEEELEELEE 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 538 EEEAKVNEIAfintlEAQNKRHDVLAKLDEYEQRLNELQEErqrrQEEK-----QARDEAVQERKRVLEAERQARVEELL 612
Cdd:COG1196 345 ELEEAEEELE-----EAEAELAEAEEALLEAEAELAEAEEE----LEELaeellEALRAAAELAAQLEELEEAEEALLER 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 613 MKRREQEARIEQQRQEKDRAREDAARERARDREERLAALSAAQQEAMEELQKKIQmKHDESSRRHMEQMEQRKEKAAELS 692
Cdd:COG1196 416 LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE-EAALLEAALAELLEELAEAAARLL 494
|
250 260
....*....|....*....|.
gi 176866331 693 SGRHANTDYAPKLTPYERKKQ 713
Cdd:COG1196 495 LLLEAEADYEGFLEGVKAALL 515
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
340-629 |
8.22e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.47 E-value: 8.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 340 EPQSMAEVLAKKEEMADRLEKANEEAIASAIAEEEQLTREIQAENSELEtDNESDFSAsigsgscgLNLDWSEM---LAD 416
Cdd:TIGR02169 713 DASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELK-ELEARIEE--------LEEDLHKLeeaLND 783
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 417 YEAR---EPWRQSTSWGDIVEEEPARPPGHGIHMHEKLSSPSRKRTIAESKKKHEEKQLKAQQLRDKLREEKTH----KL 489
Cdd:TIGR02169 784 LEARlshSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEnlngKK 863
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 490 QKLMEREKDVRKWKEELLDQRRKMMEEKLlhaefKRELQLQAIVKKAQEEEAKVnEIAFINTLEAQNKRHDVLAKLDEYE 569
Cdd:TIGR02169 864 EELEEELEELEAALRDLESRLGDLKKERD-----ELEAQLRELERKIEELEAQI-EKKRKRLSELKAKLEALEEELSEIE 937
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 176866331 570 QRLNELQEERQRRQEEK--QARDEAVQERKRVLE----------AERQARVEEL------LMKRREQ-EARIEQQRQEK 629
Cdd:TIGR02169 938 DPKGEDEEIPEEELSLEdvQAELQRVEEEIRALEpvnmlaiqeyEEVLKRLDELkekrakLEEERKAiLERIEEYEKKK 1016
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
463-712 |
1.17e-08 |
|
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: 59.75 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 463 SKKKHEEKQLKAQQlrDKLREEKTHKLQKLMEREK--DVRKWKEELLDQRRKM-MEEKLLHAEFKRELQ-LQAIVKKAQE 538
Cdd:pfam17380 285 SERQQQEKFEKMEQ--ERLRQEKEEKAREVERRRKleEAEKARQAEMDRQAAIyAEQERMAMERERELErIRQEERKREL 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 539 EEAKVNEIAFINT---------LEAQNKRHDVLAKLD-------EYEQRLNELQEERQRRQEEKQARDEAVQERKRVLEA 602
Cdd:pfam17380 363 ERIRQEEIAMEISrmrelerlqMERQQKNERVRQELEaarkvkiLEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEE 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 603 ERQ---ARVEELLMKRREQEARIEQQRQEKDRAREDAARERARDREERLAALSAAQQEAMEELQKKIQmkhDESSRRHME 679
Cdd:pfam17380 443 ERAremERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIE---EERKRKLLE 519
|
250 260 270
....*....|....*....|....*....|....
gi 176866331 680 -QMEQRKEKAAELSSGRHANTDYAPKLTPYERKK 712
Cdd:pfam17380 520 kEMEERQKAIYEEERRREAEEERRKQQEMEERRR 553
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
469-690 |
2.62e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.79 E-value: 2.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 469 EKQLKAQQLRDKLRE-EKTHKLQKLMEREKDVRKWKEELLDQRRKmmEEKLLHAEFKRELQLQAIVKKAQEEEAKVNEia 547
Cdd:COG1196 210 EKAERYRELKEELKElEAELLLLKLRELEAELEELEAELEELEAE--LEELEAELAELEAELEELRLELEELELELEE-- 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 548 fintleAQNKRHDVLAKLDEYEQRLNELQeerQRRQEEKQARDEAVQERKRVLE--AERQARVEELLMKRREQEARIEQQ 625
Cdd:COG1196 286 ------AQAEEYELLAELARLEQDIARLE---ERRRELEERLEELEEELAELEEelEELEEELEELEEELEEAEEELEEA 356
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 176866331 626 RQEKDRAREDAARERARDREERLAALSAAQQEAMEELQKKIQMKHDESSRRHMEQMEQRKEKAAE 690
Cdd:COG1196 357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
449-691 |
3.43e-08 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 57.57 E-value: 3.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 449 EKLSSPSRKRTIAESKKKHEEKQLKAQQLRDKLREEKTHKlqklMEREKDVRKWKEELLDQRRKMMEEKLLHAEFKrELQ 528
Cdd:pfam02029 96 EKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEI----REKEYQENKWSTEVRQAEEEGEEEEDKSEEAE-EVP 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 529 LQAIVKKAQEEEAKVNEIAFINTLEA--QNKRHDVLAKLDEYEQRLNELQEERQRRQEEKQARDEAVQERKRVLEAERqa 606
Cdd:pfam02029 171 TENFAKEEVKDEKIKKEKKVKYESKVflDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQ-- 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 607 RVEELLMKRREQEARIEQQRQEKDRAREDAARERARDREERLAALSAA-QQEAMEELQKKIqmKHDESSRRHMEQMEQRK 685
Cdd:pfam02029 249 KLEELRRRRQEKESEEFEKLRQKQQEAELELEELKKKREERRKLLEEEeQRRKQEEAERKL--REEEEKRRMKEEIERRR 326
|
....*.
gi 176866331 686 EKAAEL 691
Cdd:pfam02029 327 AEAAEK 332
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
328-687 |
3.77e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.23 E-value: 3.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 328 EPSKEMEKTPVIEPQSMAEVLAKKEEM--ADRLEKANEEAIASAIAEEEQLTREIQAENSELETDNESDFSASIGSGSCG 405
Cdd:PTZ00121 1519 EEAKKADEAKKAEEAKKADEAKKAEEKkkADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVM 1598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 406 LNLDWSEMLADYEAREPWRQSTSWGDIVEEEPARPPGHgiHMHEKLSSPSRKrtiAESKKKHEEK-QLKAQQLRDKLREE 484
Cdd:PTZ00121 1599 KLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVE--QLKKKEAEEKKK---AEELKKAEEEnKIKAAEEAKKAEED 1673
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 485 KtHKLQKLMEREKDVRKWKEELL---DQRRKMMEEKLLHAEFKR---ELQLQAIVKKAQEEEAKVNEiafintlEAQNKR 558
Cdd:PTZ00121 1674 K-KKAEEAKKAEEDEKKAAEALKkeaEEAKKAEELKKKEAEEKKkaeELKKAEEENKIKAEEAKKEA-------EEDKKK 1745
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 559 HDVLAKLDEYEQRLNELQEERQRRQEEKQARDEAVQERKRVLEAERQARVEELLMKRREQEARIEQQRQEKDRAREDAAR 638
Cdd:PTZ00121 1746 AEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSK 1825
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 176866331 639 ERARDREERLAALSAAQQEAMEELQKKIQMKHDESSRRHMEQMEQRKEK 687
Cdd:PTZ00121 1826 EMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEK 1874
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
456-690 |
8.12e-08 |
|
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: 55.70 E-value: 8.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 456 RKRTIAESKKKHEEKQLKAQQLRDKLREE-KTHKLQKLMERE----------KDVRKWKEE-LLDQRRKMMEEKLLHAEF 523
Cdd:pfam13868 53 RERALEEEEEKEEERKEERKRYRQELEEQiEEREQKRQEEYEeklqereqmdEIVERIQEEdQAEAEEKLEKQRQLREEI 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 524 KRELQLQAIVKKAQ-----EEEAKVNEIAFINTLEAQNKRHDVLAKLDEYEQRLNELQEERQRRQEEKQARDEAVQER-K 597
Cdd:pfam13868 133 DEFNEEQAEWKELEkeeerEEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLyQ 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 598 RVLEAERQARVEELLMKRREQEARI----EQQRQEKDRAREDAARERARDREERLAALSAAQQEAMEELQKKiQMKHDES 673
Cdd:pfam13868 213 EEQERKERQKEREEAEKKARQRQELqqarEEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKR-RMKRLEH 291
|
250
....*....|....*..
gi 176866331 674 SRRHMEQMEQRKEKAAE 690
Cdd:pfam13868 292 RRELEKQIEEREEQRAA 308
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
261-783 |
1.04e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.69 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 261 AEKPAKKDAEGWETVQRGRSMRPRAKVSPVLVHASPKDDSDKENQHVQPSPQDKSQdVREQEPPIPQEPSKEMEKTPVIE 340
Cdd:PTZ00121 1416 AKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK-ADEAKKKAEEAKKADEAKKKAEE 1494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 341 PQSMAEVLAKKEE---MADRLEKANEEAIASAIAEEEQLTREIQAENSELETDNESdfsasigsgscglnLDWSEMLADY 417
Cdd:PTZ00121 1495 AKKKADEAKKAAEakkKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADE--------------LKKAEELKKA 1560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 418 EAREPWRQSTswgdivEEEPARppGHGIHMHEKLSSPSRKRTIAESKKKHEEKQLKAQQLRdKLREE--KTHKLQKLMER 495
Cdd:PTZ00121 1561 EEKKKAEEAK------KAEEDK--NMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK-KAEEAkiKAEELKKAEEE 1631
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 496 EKDVRKWKEELLDQRRKmmEEKLLHAEFKRELQLQAIVKKAQEEEAKVNEIAfiNTLEAQNKRHDVLAKLDEYEQRLNEL 575
Cdd:PTZ00121 1632 KKKVEQLKKKEAEEKKK--AEELKKAEEENKIKAAEEAKKAEEDKKKAEEAK--KAEEDEKKAAEALKKEAEEAKKAEEL 1707
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 576 qeerqrrqeekqardeavqeRKRVLEAERQArvEELLMKRREQEARIEQ-QRQEKDRAREDAARERARDREERLAALSAA 654
Cdd:PTZ00121 1708 --------------------KKKEAEEKKKA--EELKKAEEENKIKAEEaKKEAEEDKKKAEEAKKDEEEKKKIAHLKKE 1765
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 655 QQEAMEELQKKIQM-------KHDESSRRHMEQ-MEQRKEKAAELSSGRHANTdyaPKLTPYERKKQCSLCNVVITSEVH 726
Cdd:PTZ00121 1766 EEKKAEEIRKEKEAvieeeldEEDEKRRMEVDKkIKDIFDNFANIIEGGKEGN---LVINDSKEMEDSAIKEVADSKNMQ 1842
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 176866331 727 LFSHIKGKRHQQAVRDSSSIQGRELSDEEVEHLSQKKYIVDIVTDSIVSSDNAKDGE 783
Cdd:PTZ00121 1843 LEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIE 1899
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
460-707 |
2.40e-07 |
|
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: 55.13 E-value: 2.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 460 IAESKKKHEEKQLKAQQLrdKLREEKTHKLQKL-MEREKDVRKWKEELLDQRRkmmeEKLLHAEFKRELQLQAIVK---K 535
Cdd:pfam17380 353 IRQEERKRELERIRQEEI--AMEISRMRELERLqMERQQKNERVRQELEAARK----VKILEEERQRKIQQQKVEMeqiR 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 536 AQEEEAKVNEIafiNTLEAQNKRHDVLAKLDEYEQ-------RLNELQEERQRRQEEKQARD--EAVQERKRVLEAERQA 606
Cdd:pfam17380 427 AEQEEARQREV---RRLEEERAREMERVRLEEQERqqqverlRQQEEERKRKKLELEKEKRDrkRAEEQRRKILEKELEE 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 607 RVEELLMKRREQEArIEQQRQEKDRAREDAARERARDREERlaalsaAQQEAMEELQKKIQMKHDESSRRHMEQMEQRKE 686
Cdd:pfam17380 504 RKQAMIEEERKRKL-LEKEMEERQKAIYEEERRREAEEERR------KQQEMEERRRIQEQMRKATEERSRLEAMERERE 576
|
250 260
....*....|....*....|.
gi 176866331 687 KAAELSSGRHANTDYaPKLTP 707
Cdd:pfam17380 577 MMRQIVESEKARAEY-EATTP 596
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
496-705 |
1.94e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.61 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 496 EKDVRKWKEELLDQRRKM--MEEKLLHAEFKRELqLQAIVKKAQEEEAKVNEIAFINTL-------EAQNKRHDVLAKLD 566
Cdd:COG4913 220 EPDTFEAADALVEHFDDLerAHEALEDAREQIEL-LEPIRELAERYAAARERLAELEYLraalrlwFAQRRLELLEAELE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 567 EYEQRLNELqeerQRRQEEKQARDEAVQERKRVLEAERQ----ARVEELLMKRREQEARIEQ-----QRQEKDRAREDAA 637
Cdd:COG4913 299 ELRAELARL----EAELERLEARLDALREELDELEAQIRgnggDRLEQLEREIERLERELEErerrrARLEALLAALGLP 374
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 176866331 638 RERARDREERLAALSAAQQEAMEELQKKIQMKHDESSRRHMEQMEQRKEKAAELSSGRHANTDYAPKL 705
Cdd:COG4913 375 LPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARL 442
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
452-690 |
2.29e-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: 52.37 E-value: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 452 SSPSRKRTIAESK---KKHEEKQLKAQQlrdKLREEKTHklqklMEREKDVRKWKEELLD----QRRKMMEEKLLHAEfK 524
Cdd:TIGR02168 152 AKPEERRAIFEEAagiSKYKERRKETER---KLERTREN-----LDRLEDILNELERQLKslerQAEKAERYKELKAE-L 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 525 RELQLQAIVKKAQEEEAKVNEIAFInTLEAQNKRHDVLAKLDEYEQRLNELqeerqrrQEEKQARDEAVQERKRVLEA-- 602
Cdd:TIGR02168 223 RELELALLVLRLEELREELEELQEE-LKEAEEELEELTAELQELEEKLEEL-------RLEVSELEEEIEELQKELYAla 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 603 ERQARVEELLMKRREQEARIEQQRQEKdrareDAARERARDREERLAALSAAQQEAMEELQKKIQMKHDESSRRHMEQ-- 680
Cdd:TIGR02168 295 NEISRLEQQKQILRERLANLERQLEEL-----EAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELee 369
|
250
....*....|
gi 176866331 681 MEQRKEKAAE 690
Cdd:TIGR02168 370 LESRLEELEE 379
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
455-697 |
2.97e-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: 51.98 E-value: 2.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 455 SRKRTIAESKKKHEEKQLKAQQLRDKLREekthKLQKLMEREKDVRKWKEELLDQRRKMMEEKL----LHAEFKRELQLQ 530
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAE----LRKELEELEEELEQLRKELEELSRQISALRKdlarLEAEVEQLEERI 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 531 AIVKKAQEEEAKVNEIAFINTLEAQNKRHDVLAKLDEYEQRLNELQEERQRRQEEKQARDEAVQERKRVLeAERQARVEE 610
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA-ANLRERLES 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 611 LLMKRREQEARIEQQRQEKdraredaarERARDREERLAALSAAQQEAMEELQKKIQmKHDESSRRHMEQMEQRKEKAAE 690
Cdd:TIGR02168 829 LERRIAATERRLEDLEEQI---------EELSEDIESLAAEIEELEELIEELESELE-ALLNERASLEEALALLRSELEE 898
|
....*..
gi 176866331 691 LSSGRHA 697
Cdd:TIGR02168 899 LSEELRE 905
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
363-872 |
3.40e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.07 E-value: 3.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 363 EEAIASAIAEEEQLTREIQAENSELETDNESDFSASIGSGScGLNLDWSEMlaDYEAREPWRQSTSWGDIVEE-EPARPP 441
Cdd:PTZ00121 1030 EELTEYGNNDDVLKEKDIIDEDIDGNHEGKAEAKAHVGQDE-GLKPSYKDF--DFDAKEDNRADEATEEAFGKaEEAKKT 1106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 442 GHGIHMHEKLSSPSRKRtiAESKKKHEEKQlKAQQLR--DKLREEKTHKLQKLMEREKDVRKWKEELLDQRRKMMEEKLL 519
Cdd:PTZ00121 1107 ETGKAEEARKAEEAKKK--AEDARKAEEAR-KAEDARkaEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARK 1183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 520 HAEFKR--ELQLQAIVKKAQ-----EEEAKVNEI-AFINTLEAQNKRHDVLAKLDEYEQRLNELQEERQRRQEEKQARDE 591
Cdd:PTZ00121 1184 AEEVRKaeELRKAEDARKAEaarkaEEERKAEEArKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMA 1263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 592 AVQERKRVLEAERQARVEELLMKRREQEARIEQQRQEKDRAREDAARERARDREERLAALSAAQQEAMEELQKKIQ--MK 669
Cdd:PTZ00121 1264 HFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEeaKK 1343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 670 HDESSRRHMEQMEQRKEKAAELSSGRHANTDYAPKLTPYERKKqcslcnvviTSEVHLFSHIKgKRHQQAVRDSSSIQGR 749
Cdd:PTZ00121 1344 AAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKK---------AEEKKKADEAK-KKAEEDKKKADELKKA 1413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 750 ELSDEEVEHLSQKkyivdivTDSIVSSDNAKDGEERQKarkkakklrarmnsRAKEYETCMEAKSQTSDSPYKAKLQRLV 829
Cdd:PTZ00121 1414 AAAKKKADEAKKK-------AEEKKKADEAKKKAEEAK--------------KADEAKKKAEEAKKAEEAKKKAEEAKKA 1472
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 176866331 830 KDLVKQQQGQDSGQWASNKVSGLDRTLGEISRILEKQNNADQV 872
Cdd:PTZ00121 1473 DEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEA 1515
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
457-691 |
3.92e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 50.69 E-value: 3.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 457 KRTIAESKKKHEEKQLKAQQLRDKLREEKTHKLQKLMEREKD-------VRKWKEE-LLDQRRKMMEEKLLHAEFKRELQ 528
Cdd:pfam13868 58 EEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEreqmdeiVERIQEEdQAEAEEKLEKQRQLREEIDEFNE 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 529 LQAIVKKAQEEEAKVNEIAFINTLEAQNKRhdvlakLDEYEQRLNELQEERQRRQEEKQARDEAVQERKRVLEAERQARV 608
Cdd:pfam13868 138 EQAEWKELEKEEEREEDERILEYLKEKAER------EEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLY 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 609 EELLMKRREQEARIEQQRQEKDRAREDAARERARDREERLAALSAAQQEAMEELQKKIQMKHDEssrrhMEQMEQRKEKA 688
Cdd:pfam13868 212 QEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEE-----IEQEEAEKRRM 286
|
...
gi 176866331 689 AEL 691
Cdd:pfam13868 287 KRL 289
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
456-690 |
5.82e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 49.92 E-value: 5.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 456 RKRTIAESKKKHEEKQLKAQQLRDKLREEKTHKLQKLMEREKDVRKWKEELLDQRRKMMEEK-----LLHAEFKRE-LQL 529
Cdd:pfam13868 24 RDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEReqkrqEEYEEKLQErEQM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 530 QAIVKKAQ-EEEAKV--NEIAFINTLEAQNKRHDVLAKLDEYE-QRLNELQEERQRRQEEKQARDEAVQERKRVLEAERQ 605
Cdd:pfam13868 104 DEIVERIQeEDQAEAeeKLEKQRQLREEIDEFNEEQAEWKELEkEEEREEDERILEYLKEKAEREEEREAEREEIEEEKE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 606 ARVEEL---LMKRREQEARIEQQRQEKDRAredaarerardreerlAALSAAQQEAMEELQKKIQMKHDESSRRHMEQME 682
Cdd:pfam13868 184 REIARLraqQEKAQDEKAERDELRAKLYQE----------------EQERKERQKEREEAEKKARQRQELQQAREEQIEL 247
|
....*...
gi 176866331 683 QRKEKAAE 690
Cdd:pfam13868 248 KERRLAEE 255
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
461-629 |
7.12e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 49.92 E-value: 7.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 461 AESKKKHEEKQLKAQQLRDKLREEKTHK------LQKLMEREKDvRKWKE-ELLDQRRKMMEEKLLHAEFKRELQLQaiv 533
Cdd:pfam13868 173 AEREEIEEEKEREIARLRAQQEKAQDEKaerdelRAKLYQEEQE-RKERQkEREEAEKKARQRQELQQAREEQIELK--- 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 534 KKAQEEEAKVNEIAFINTLEAQnkrhdvlAKLDEYEQRLNELQEERQRRQEEKQARDeaVQERKRVLEAERQARVEELLM 613
Cdd:pfam13868 249 ERRLAEEAEREEEEFERMLRKQ-------AEDEEIEQEEAEKRRMKRLEHRRELEKQ--IEEREEQRAAEREEELEEGER 319
|
170
....*....|....*....
gi 176866331 614 KRREQE---ARIEQQRQEK 629
Cdd:pfam13868 320 LREEEAerrERIEEERQKK 338
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
347-700 |
8.68e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.45 E-value: 8.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 347 VLAKKEEMADRLEKANEEAIASAIAEEEQLTREIQAENSELETDNE--SDFSASIgsgscglnldwsEMLADYEAREpwr 424
Cdd:TIGR02169 227 ELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQllEELNKKI------------KDLGEEEQLR--- 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 425 qstswgdiVEEEparppghgihMHEKLSSPSR-KRTIAESK---KKHEEKQLKAQQLRDKLREEKTHKLQKLMEREKDVR 500
Cdd:TIGR02169 292 --------VKEK----------IGELEAEIASlERSIAEKErelEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRD 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 501 KWKEELLDQRRKMMEekllhaefkrelqlqaIVKKAQEEEAKVNEiafinTLEAQNKRHDvlaKLDEYEQRLNELQEERQ 580
Cdd:TIGR02169 354 KLTEEYAELKEELED----------------LRAELEEVDKEFAE-----TRDELKDYRE---KLEKLKREINELKRELD 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 581 RRQEEKQARDEAVQERKRVLE------AERQARVEELLMKRREQEARIEQQRQEKDRAREDAArerardreerlaalsaA 654
Cdd:TIGR02169 410 RLQEELQRLSEELADLNAAIAgieakiNELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELY----------------D 473
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 176866331 655 QQEAMEELQKKIqmkhdESSRRHMEQMEQRKEKAAELSSGRHANTD 700
Cdd:TIGR02169 474 LKEEYDRVEKEL-----SKLQRELAEAEAQARASEERVRGGRAVEE 514
|
|
| ZnF_U1 |
smart00451 |
U1-like zinc finger; Family of C2H2-type zinc fingers, present in matrin, U1 small nuclear ... |
710-741 |
8.90e-06 |
|
U1-like zinc finger; Family of C2H2-type zinc fingers, present in matrin, U1 small nuclear ribonucleoprotein C and other RNA-binding proteins.
Pssm-ID: 197732 [Multi-domain] Cd Length: 35 Bit Score: 43.78 E-value: 8.90e-06
10 20 30
....*....|....*....|....*....|..
gi 176866331 710 RKKQCSLCNVVITSEVHLFSHIKGKRHQQAVR 741
Cdd:smart00451 2 GGFYCKLCNVTFTDEISVEAHLKGKKHKKNVK 33
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
457-690 |
9.38e-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: 50.44 E-value: 9.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 457 KRTIAESKKKHEEKQLKAQQLRDKLrEEKTHKLQKL------MEREKDVRKWKEELLDQRRKMMEEKLLHAEFKRELQLQ 530
Cdd:TIGR02168 259 TAELQELEEKLEELRLEVSELEEEI-EELQKELYALaneisrLEQQKQILRERLANLERQLEELEAQLEELESKLDELAE 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 531 AIVK-KAQEEEAKVNEIAFINTL-EAQNKRHDVLAKLDEYEQRLNELQEE-RQRRQEEKQARDEAVQERKRV--LEAER- 604
Cdd:TIGR02168 338 ELAElEEKLEELKEELESLEAELeELEAELEELESRLEELEEQLETLRSKvAQLELQIASLNNEIERLEARLerLEDRRe 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 605 --QARVEELLMKRREQEARIEQQRQEKDRAREDAARERARDREERLAALSAAQQEAMEELQKKIQMKHDESSRRHM-EQM 681
Cdd:TIGR02168 418 rlQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSlERL 497
|
....*....
gi 176866331 682 EQRKEKAAE 690
Cdd:TIGR02168 498 QENLEGFSE 506
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
462-691 |
1.16e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 49.97 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 462 ESKKKHEEKQLKAQQLRDKLREEKthKLQKLMEREKD-----VRKWKEELLDQRRKMMEEKLLHAEFKRELQLQaIVKKA 536
Cdd:pfam02463 174 ALKKLIEETENLAELIIDLEELKL--QELKLKEQAKKaleyyQLKEKLELEEEYLLYLDYLKLNEERIDLLQEL-LRDEQ 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 537 QEEEAKVNEIAFINTLEAQNKRhdvlakldeyEQRLNELQEERQRRQEEKQARDEAVQERKRvleaeRQARVEELLMKRR 616
Cdd:pfam02463 251 EEIESSKQEIEKEEEKLAQVLK----------ENKEEEKEKKLQEEELKLLAKEEEELKSEL-----LKLERRKVDDEEK 315
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 176866331 617 EQEARIEQQRQEKDRAREDAArerardreerlaalSAAQQEAMEELQKKIQMKHDEssrrhMEQMEQRKEKAAEL 691
Cdd:pfam02463 316 LKESEKEKKKAEKELKKEKEE--------------IEELEKELKELEIKREAEEEE-----EEELEKLQEKLEQL 371
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
457-690 |
1.36e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 457 KRTIAESKKKHEEKQLKAQQLRDKLRE---EKTHKLQKLMEREKDVRKWKEELLDQRRKMMEEKLLHAEF-KRELQLQAI 532
Cdd:PRK03918 171 IKEIKRRIERLEKFIKRTENIEELIKEkekELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIeELEKELESL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 533 VKKAQEEEAKVNEI-AFINTLEAQnkrhdvLAKLDEYEQRLNELQEERQRRQEEKQARDEAVQERKRV------LEAERQ 605
Cdd:PRK03918 251 EGSKRKLEEKIRELeERIEELKKE------IEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIekrlsrLEEEIN 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 606 ArVEELLMKRREQEARIEQQRQEKDRAREDAARERARDREERLAalsAAQQEAMEELQKKIQMKHDESSRRHMEQMEQRK 685
Cdd:PRK03918 325 G-IEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEA---KAKKEELERLKKRLTGLTPEKLEKELEELEKAK 400
|
....*
gi 176866331 686 EKAAE 690
Cdd:PRK03918 401 EEIEE 405
|
|
| zf-met |
pfam12874 |
Zinc-finger of C2H2 type; This is a zinc-finger domain with the CxxCx(12)Hx(6)H motif, found ... |
714-736 |
1.40e-05 |
|
Zinc-finger of C2H2 type; This is a zinc-finger domain with the CxxCx(12)Hx(6)H motif, found in multiple copies in a wide range of proteins from plants to metazoans. Some member proteins, particularly those from plants, are annotated as being RNA-binding.
Pssm-ID: 463736 [Multi-domain] Cd Length: 25 Bit Score: 42.87 E-value: 1.40e-05
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
461-629 |
1.60e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 48.65 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 461 AESKKKHEEKQLKAQQLRDKLREEKTHKLQKLMEREKdvrkwkeelldQRRKMMEEKLLHAEFKRELQLQAivKKAQEEE 540
Cdd:PRK09510 72 KSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEK-----------ERLAAQEQKKQAEEAAKQAALKQ--KQAEEAA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 541 AKVNEIAFINTlEAQNKRHDVLAKLDEYEQRLNElqeerqrrqeEKQARDEAVQERKRVLEAERQARVEELLMKRREQEA 620
Cdd:PRK09510 139 AKAAAAAKAKA-EAEAKRAAAAAKKAAAEAKKKA----------EAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEA 207
|
....*....
gi 176866331 621 RIEQQRQEK 629
Cdd:PRK09510 208 KKKAAAEAK 216
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
429-629 |
1.83e-05 |
|
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: 48.30 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 429 WGDIVEEEPARPPGHGIHMHEKLSSPSRKRTIAESKKKHEEKQLKAQQLRDKLREEKTHKLQKLMEREK-DVRKWKEELL 507
Cdd:TIGR02794 20 LGSLYHSVKPEPGGGAEIIQAVLVDPGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQaRQKELEQRAA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 508 DQRRKMMEEKllHAEFKRELQLQAIVKKA-QEEEAKVNEIAfintlEAQNKRHDVLAKLDEYEQRLNElqeERQRRQEEK 586
Cdd:TIGR02794 100 AEKAAKQAEQ--AAKQAEEKQKQAEEAKAkQAAEAKAKAEA-----EAERKAKEEAAKQAEEEAKAKA---AAEAKKKAE 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 176866331 587 QARDEAVQERKRVLEAERQARVEELLMKRREQEARIEQQRQEK 629
Cdd:TIGR02794 170 EAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAK 212
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
258-690 |
2.17e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.37 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 258 YIPAEKPAKKDAEGWETVQRGRSMRPRAKVSPV--LVHASPKDDSDKENQHVQPSPQ-DKSQDVREQEPPIPQEPSKEME 334
Cdd:PTZ00121 1076 YKDFDFDAKEDNRADEATEEAFGKAEEAKKTETgkAEEARKAEEAKKKAEDARKAEEaRKAEDARKAEEARKAEDAKRVE 1155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 335 KTPVIEPQSMAEVlAKKEEMADRLE---KANEEAIASAIAEEEQLTREIQAENSELETDNESDFSASIGSGSCGLNlDWS 411
Cdd:PTZ00121 1156 IARKAEDARKAEE-ARKAEDAKKAEaarKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVK-KAE 1233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 412 EMLADYEAREPWRQSTSWGDIVEEEPARPPGHGIHMHEKLSSPSRKrtiAESKKKHEEKQlKAQQLRdklREEKTHKLQK 491
Cdd:PTZ00121 1234 EAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARK---ADELKKAEEKK-KADEAK---KAEEKKKADE 1306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 492 LMEREKDVRKwkeelLDQRRKMMEEKLLHAEfkrELQLQAIVKKAQEEEAKVNEIAFINTLEAQNKRhdvlAKLDEYEQr 571
Cdd:PTZ00121 1307 AKKKAEEAKK-----ADEAKKKAEEAKKKAD---AAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEK----AEAAEKKK- 1373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 572 lnelqeerqrrQEEKQARDEA---VQERKRVLEAERQA-----RVEELLMKRREQEARIE-QQRQEKDRAREDAARERAR 642
Cdd:PTZ00121 1374 -----------EEAKKKADAAkkkAEEKKKADEAKKKAeedkkKADELKKAAAAKKKADEaKKKAEEKKKADEAKKKAEE 1442
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 176866331 643 DREERLAALSAAQQEAMEELQKKIQ--MKHDESSRRHME--QMEQRKEKAAE 690
Cdd:PTZ00121 1443 AKKADEAKKKAEEAKKAEEAKKKAEeaKKADEAKKKAEEakKADEAKKKAEE 1494
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
454-690 |
2.71e-05 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 48.11 E-value: 2.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 454 PSRKRTIAE---SKKKHEEKQLKAQQLRDKLREEKTHKLQKLMEREKDVRKWkeeLLDQRRKMMEEKLlhAEFKRELQlq 530
Cdd:pfam15558 3 PERDRKIAAlmlARHKEEQRMRELQQQAALAWEELRRRDQKRQETLERERRL---LLQQSQEQWQAEK--EQRKARLG-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 531 aivkkaQEEEAKVnEIAFINTLEAQNKRhdvLAKLDEYE-QRLNELQEERQRRQEEKQARDEAVQERKRVLEAERQArvE 609
Cdd:pfam15558 76 ------REERRRA-DRREKQVIEKESRW---REQAEDQEnQRQEKLERARQEAEQRKQCQEQRLKEKEEELQALREQ--N 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 610 ELLMKRREQEARIEQQRQEKDRAREDAARERARDREERLAALSAAQQEAMEELQKK--IQMKHDESSRRHMEQMEQR--- 684
Cdd:pfam15558 144 SLQLQERLEEACHKRQLKEREEQKKVQENNLSELLNHQARKVLVDCQAKAEELLRRlsLEQSLQRSQENYEQLVEERhre 223
|
....*..
gi 176866331 685 -KEKAAE 690
Cdd:pfam15558 224 lREKAQK 230
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
464-623 |
3.06e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.24 E-value: 3.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 464 KKKHEEKQLKAQQLRDKLREE-----KTHKLQKLMEREKDVRKWKEElLDQRRKMMEEKLLHAEfKRELQLQAIVKKAQE 538
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEakkeaEAIKKEALLEAKEEIHKLRNE-FEKELRERRNELQKLE-KRLLQKEENLDRKLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 539 EEAKVNEiafintlEAQNKRHDVLAKLDEYEQRLNELqeerqrrqeeKQARDEAVQERKRV--LEAErQARveELLMKRR 616
Cdd:PRK12704 104 LLEKREE-------ELEKKEKELEQKQQELEKKEEEL----------EELIEEQLQELERIsgLTAE-EAK--EILLEKV 163
|
....*..
gi 176866331 617 EQEARIE 623
Cdd:PRK12704 164 EEEARHE 170
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
510-691 |
4.27e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.85 E-value: 4.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 510 RRKMMEEKLLHAEFKRELQLQAIVKKAQE--EEAKvneiafintLEAQNKRHDVLAKLD-EYEQRLNELqeerqrrqeek 586
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEEAKKEAEAikKEAL---------LEAKEEIHKLRNEFEkELRERRNEL----------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 587 QARDEAVQERKRVLEaerqaRVEELLMKRreqEARIEQQRQEKDRAREDAARERARdreerlaaLSAAQQEAMEELQKKI 666
Cdd:PRK12704 85 QKLEKRLLQKEENLD-----RKLELLEKR---EEELEKKEKELEQKQQELEKKEEE--------LEELIEEQLQELERIS 148
|
170 180
....*....|....*....|....*.
gi 176866331 667 QMKHDESSRRHMEQMEQR-KEKAAEL 691
Cdd:PRK12704 149 GLTAEEAKEILLEKVEEEaRHEAAVL 174
|
|
| Stathmin |
pfam00836 |
Stathmin family; The Stathmin family of proteins play an important role in the regulation of ... |
440-546 |
5.61e-05 |
|
Stathmin family; The Stathmin family of proteins play an important role in the regulation of the microtubule cytoskeleton. They regulate microtubule dynamics by promoting depolymerization of microtubules and/or preventing polymerization of tubulin heterodimers.
Pssm-ID: 459956 [Multi-domain] Cd Length: 136 Bit Score: 44.26 E-value: 5.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 440 PPGHGIHMHEKLSSPSRKRTIAESKkkheEKQLKAQQLRDKLRE-EKTHKLQKLMEREKDVRKWKEELLDQRRKMMEEKL 518
Cdd:pfam00836 23 PPSVNAAPPKLSLSPKKKDSSLEEI----QKKLEAAEERRKSLEaQKLKQLAEKREKEEEALQKADEENNNFSKMAEEKL 98
|
90 100 110
....*....|....*....|....*....|..
gi 176866331 519 LHA----EFKRELQLQAIVKKAQEEEAKVNEI 546
Cdd:pfam00836 99 KQKmeayKENREAQIAALKEKLKEKEKHVEEV 130
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
449-628 |
9.24e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 9.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 449 EKLSSPS-RKRTIAESKKKHEEKQLKAQQLRDKLREEKTHKLQKLMEREKDVRKWKEELLDQRRKMmeekllhaefKREL 527
Cdd:COG4717 56 DELFKPQgRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL----------EKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 528 QLQAIVKKAQEEEAKVNEIAfintleaqnkrhDVLAKLDEYEQRLNELQEERQRRQEEKQARDEAVQERKRVLEAERQAR 607
Cdd:COG4717 126 QLLPLYQELEALEAELAELP------------ERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEE 193
|
170 180
....*....|....*....|.
gi 176866331 608 VEELLMKRREQEARIEQQRQE 628
Cdd:COG4717 194 LQDLAEELEELQQRLAELEEE 214
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
457-629 |
1.05e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 46.74 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 457 KRTIAESKKKHEEKQLKAQQLRDKLrEEKTHKLQKLmerEKDVRKWKEELLDQRRKM--MEEKLLHaefKRELQLQAIVK 534
Cdd:PRK00409 508 KKLIGEDKEKLNELIASLEELEREL-EQKAEEAEAL---LKEAEKLKEELEEKKEKLqeEEDKLLE---EAEKEAQQAIK 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 535 KAQEEEAKVneIAFINTLEAQNKRHDVLAKLDEYEQRLNELQEERQRRQEEKQARDEAVQERKRV-------------LE 601
Cdd:PRK00409 581 EAKKEADEI--IKELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELKVGDEVkylslgqkgevlsIP 658
|
170 180 190
....*....|....*....|....*....|.
gi 176866331 602 AERQARVEELLMKRREQEA---RIEQQRQEK 629
Cdd:PRK00409 659 DDKEAIVQAGIMKMKVPLSdleKIQKPKKKK 689
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
457-629 |
1.32e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.31 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 457 KRTIAESKKKHE----EKQLKAQQLRDKLREE-------KTHKLQK----LMEREKDVRKwKEELLDQRrkmmEEKLLHA 521
Cdd:PRK12704 41 KRILEEAKKEAEaikkEALLEAKEEIHKLRNEfekelreRRNELQKlekrLLQKEENLDR-KLELLEKR----EEELEKK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 522 EFKRELQLQAIVKKAQEEEAKVNEiafintleaQNKRHDVLAKLDeyeqrlnelqeerqrrqeekqaRDEAvqeRKRVLE 601
Cdd:PRK12704 116 EKELEQKQQELEKKEEELEELIEE---------QLQELERISGLT----------------------AEEA---KEILLE 161
|
170 180 190
....*....|....*....|....*....|
gi 176866331 602 -AERQARVE-ELLMKRREQEARIEQQRQEK 629
Cdd:PRK12704 162 kVEEEARHEaAVLIKEIEEEAKEEADKKAK 191
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
457-629 |
2.18e-04 |
|
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: 45.33 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 457 KRTIAESKKKHEEKQLKAQQLRdklrEEKTHKLQKLMEREKDVRKWKEELLDQRRKMMEEKLLHAEFKRELQLQAIVKKA 536
Cdd:pfam15709 346 RRLEVERKRREQEEQRRLQQEQ----LERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERA 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 537 --QEEE--AKVNEIAfintleaQNKRHDVLAKLDEYEQRLNELQEERQRRQEE--KQARDEAVQERKRVLEAERQARVEE 610
Cdd:pfam15709 422 rqQQEEfrRKLQELQ-------RKKQQEEAERAEAEKQRQKELEMQLAEEQKRlmEMAEEERLEYQRQKQEAEEKARLEA 494
|
170 180
....*....|....*....|....*
gi 176866331 611 LLMKRREQEA------RIEQQRQEK 629
Cdd:pfam15709 495 EERRQKEEEAarlaleEAMKQAQEQ 519
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
488-691 |
4.47e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 4.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 488 KLQKlmEREKDVRKW--KEELLDQRRKMMEEKLLHAEfKRELQLQAIVKKAQEEEAKVNEI-AFINTLEAQNKRHDVLAK 564
Cdd:COG4717 50 RLEK--EADELFKPQgrKPELNLKELKELEEELKEAE-EKEEEYAELQEELEELEEELEELeAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 565 LDEYEQRLNELqeerqrrqeekQARDEAVQERKRVLEAERQARvEELLMKRREQEARIEQ---QRQEKDRAREDAARERA 641
Cdd:COG4717 127 LLPLYQELEAL-----------EAELAELPERLEELEERLEEL-RELEEELEELEAELAElqeELEELLEQLSLATEEEL 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 176866331 642 RDREERLAALSAAQQEAMEELqKKIQMKHDESSRRhMEQMEQRKEKAAEL 691
Cdd:COG4717 195 QDLAEELEELQQRLAELEEEL-EEAQEELEELEEE-LEQLENELEAAALE 242
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
456-575 |
4.54e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.93 E-value: 4.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 456 RKRTIAESKKKHEEKQLKAQQLRDKLREEKTHKLQKLMEREKDVRKWKEELLDQRRKMMEEKLLHAEFK-RELQLQAIVK 534
Cdd:COG1196 659 GGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEeQLEAEREELL 738
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 176866331 535 KAQEEEAKVNEIAFINTLEAQNKRHDVLAKLDEYEQRLNEL 575
Cdd:COG1196 739 EELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
464-697 |
4.81e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.54 E-value: 4.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 464 KKKHE-EKQLKAQQ-----LRDkLREEKTHKLQKLmEREKDV----RKWKEELlDQRRKmmeEKLLHAEFKRELQLQAIV 533
Cdd:COG1196 172 ERKEEaERKLEATEenlerLED-ILGELERQLEPL-ERQAEKaeryRELKEEL-KELEA---ELLLLKLRELEAELEELE 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 534 KKAQEEEAKVNEiafintLEAQNKRHDvlAKLDEYEQRLNELqeerqrrqeekQARDEAVQERkrvlEAERQARVEELlm 613
Cdd:COG1196 246 AELEELEAELEE------LEAELAELE--AELEELRLELEEL-----------ELELEEAQAE----EYELLAELARL-- 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 614 krrEQEARIEQQR-------QEKDRAREDAARERARDREERLAALSAAQQEAMEELQKKIQMKHDESSRRHMEQmEQRKE 686
Cdd:COG1196 301 ---EQDIARLEERrreleerLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE-AELAE 376
|
250
....*....|.
gi 176866331 687 KAAELSSGRHA 697
Cdd:COG1196 377 AEEELEELAEE 387
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
454-669 |
5.54e-04 |
|
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: 44.17 E-value: 5.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 454 PSRKRTIAESKKKHEEKQLKAQQLRDKLREEKTHKLQ-----KLMEREKDVRKWKEELldQRRKMMEEKLLHAEFKRELQ 528
Cdd:pfam15709 311 SEEERSEEDPSKALLEKREQEKASRDRLRAERAEMRRleverKRREQEEQRRLQQEQL--ERAEKMREELELEQQRRFEE 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 529 LQAIVKKAQEEEAKVNEIAFINTLEAQNKRHDVLAKLDEYEQRLNELQEERQRRQEEkqaRDEAVQERKRVLEaERQARV 608
Cdd:pfam15709 389 IRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAE---RAEAEKQRQKELE-MQLAEE 464
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 176866331 609 EELLMKRREQEaRIEQQRQEKDRAREDAARERARDREERLAAlsaaqQEAMEELQKKIQMK 669
Cdd:pfam15709 465 QKRLMEMAEEE-RLEYQRQKQEAEEKARLEAEERRQKEEEAA-----RLALEEAMKQAQEQ 519
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
512-690 |
5.99e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 43.75 E-value: 5.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 512 KMMEEKLLHAEFKRELQLQAIVKKAQEEEAKVNEIAFINTLEAQNKRHdvLAKLDEYEQRLNElqeerqrrqEEKQARDE 591
Cdd:pfam13868 9 RELNSKLLAAKCNKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERA--LEEEEEKEEERKE---------ERKRYRQE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 592 AVQ-----ERKRVLEAERQAR----VEELLMKRREQEARIEQQRQEKDRAREDAArerardreerlaALSAAQQEAMEEL 662
Cdd:pfam13868 78 LEEqieerEQKRQEEYEEKLQereqMDEIVERIQEEDQAEAEEKLEKQRQLREEI------------DEFNEEQAEWKEL 145
|
170 180
....*....|....*....|....*...
gi 176866331 663 QKKIQMKHDESSRRHMEQMEQRKEKAAE 690
Cdd:pfam13868 146 EKEEEREEDERILEYLKEKAEREEEREA 173
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
449-875 |
1.01e-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: 43.81 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 449 EKLSSPSRKRTIAESKKKHEEKQLKAQQLRDKLREEKTHkLQKLMEREKDVRKWKEELLDQRRKMMEEKLLHAEFKRELQ 528
Cdd:pfam02463 301 ELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEE-LEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKK 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 529 LQAIVKKAQEEEAKVNEIAFINTLEAQNKRHDVLA--KLDEYEQRLNELQEERQRRQEEKQARDEAVQERKrvLEAERQA 606
Cdd:pfam02463 380 KLESERLSSAAKLKEEELELKSEEEKEAQLLLELArqLEDLLKEEKKEELEILEEEEESIELKQGKLTEEK--EELEKQE 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 607 RVEELLMKRREQEARIEQQRQEKDRAREDAARERARDREERLAALSAAQQEAMEELQKKIQMKHDESSRRH--------- 677
Cdd:pfam02463 458 LKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHgrlgdlgva 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 678 ------------MEQMEQRKEKAAELSSGRHANTDYAPKLTPYERKKQCSLCNVVITSEVHLFSHIKGKRHQQAVRDSSS 745
Cdd:pfam02463 538 venykvaistavIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADE 617
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 746 IQGRELSDEEVEHLSQKKYIVDIVTDSIVSSDNAKDGEERQKARKKAKKLRARMNSRAKEYETCMEAKSQTSDSPYKAKL 825
Cdd:pfam02463 618 DDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRR 697
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 176866331 826 QrlvkDLVKQQQGQDSGQWASNKVSGLDRTLGEISRILEKQNNADQVAFQ 875
Cdd:pfam02463 698 Q----LEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQ 743
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
469-693 |
1.01e-03 |
|
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: 43.21 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 469 EKQLKAQQLRDKLREEKTHKLQKLMEREKDVRKWKEELLDQRRKMMEekllhaefkRELQLQAIVKKAQEEEAKVNEIAF 548
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAA---------LARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 549 -INTLEAQ-NKRHDVLAKLDEYEQRLNELQEERQRRQEEKQARDEAVQERKRVLEAERQARVEELLMKRRE---QEARIE 623
Cdd:COG4942 91 eIAELRAElEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAElaaLRAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 624 QQRQEKdrareDAARERARDREERLAALSAAQQEAMEELQKKIQmkhdessrRHMEQMEQRKEKAAELSS 693
Cdd:COG4942 171 AERAEL-----EALLAELEEERAALEALKAERQKLLARLEKELA--------ELAAELAELQQEAEELEA 227
|
|
| CCDC47 |
pfam07946 |
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ... |
586-669 |
1.31e-03 |
|
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of the PAT complex, an endoplasmic reticulum (ER)-resident membrane multiprotein complex that facilitates multi-pass membrane proteins insertion into membranes. The PAT complex, formed by CCDC47 and Asterix proteins, acts as an intramembrane chaperone by directly interacting with nascent transmembrane domains (TMDs), releasing its substrates upon correct folding, and is needed for optimal biogenesis of multi-pass membrane proteins. CCDC47 is required to maintain the stability of Asterix. CCDC47 is associated with various membrane-associated processes and is component of a ribosome-associated ER translocon complex involved in multi-pass membrane protein transport into the ER membrane and biogenesis. It is also involved in the regulation of calcium ion homeostasis in the ER, being also required for proper protein degradation via the ERAD (ER-associated degradation) pathway.
Pssm-ID: 462322 Cd Length: 323 Bit Score: 42.55 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 586 KQARDEAVQERKRVLEAERQarvEELLMKRREQEARIEQQRqekdraredaarerardreerLAALSAAQQEAMEELQKK 665
Cdd:pfam07946 263 KKTREEEIEKIKKAAEEERA---EEAQEKKEEAKKKEREEK---------------------LAKLSPEEQRKYEEKERK 318
|
....
gi 176866331 666 IQMK 669
Cdd:pfam07946 319 KEQR 322
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
468-688 |
1.38e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.08 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 468 EEKQLKAQQLRDKLREEKTHKLQKLMEREKDVRKWKEE-----------LLDQRRKMMEEKLLHAEFKREL------QLQ 530
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKnglvdlseeakLLLQQLSELESQLAEARAELAEaearlaALR 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 531 AIVKKAQEEEAKVNEIAFINTLEAQnkRHDVLAKLDEYEQRLNELQEERQRRQEEKQARDEAVQERKRVLEAERQARVEE 610
Cdd:COG3206 247 AQLGSGPDALPELLQSPVIQQLRAQ--LAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEA 324
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 176866331 611 LLMKRREQEARIEQQRQEkdraredaarerardreerLAALSAAQQEaMEELQKKIqmkhdESSRRHMEQMEQRKEKA 688
Cdd:COG3206 325 LQAREASLQAQLAQLEAR-------------------LAELPELEAE-LRRLEREV-----EVARELYESLLQRLEEA 377
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
345-700 |
1.48e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 345 AEVLAKKEEMADRLEKANE------EAIASAIAEEEQLTREIQ---AENSELETDNESdfsasiGSGSCGLNLDWSEMLA 415
Cdd:PRK02224 240 DEVLEEHEERREELETLEAeiedlrETIAETEREREELAEEVRdlrERLEELEEERDD------LLAEAGLDDADAEAVE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 416 DYEAREPWRQSTSWGDIVEEEPArppghgIHMHEKLSSPSRKRtIAESKKKHEEKQLKAQQLRDKL---REEKTHKLQKL 492
Cdd:PRK02224 314 ARREELEDRDEELRDRLEECRVA------AQAHNEEAESLRED-ADDLEERAEELREEAAELESELeeaREAVEDRREEI 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 493 MEREKDVRKWKEEL---------LDQRRKMMEEKL--LHAefkRELQLQAIVKKAQEEEAKVNEIafintLEAQN----- 556
Cdd:PRK02224 387 EELEEEIEELRERFgdapvdlgnAEDFLEELREERdeLRE---REAELEATLRTARERVEEAEAL-----LEAGKcpecg 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 557 ---KRHDVLAKLDEYEQRLNELQEERQRRQEEKQARDEAVQERKRVLEAERqaRVEELLMKRREQEARIEQQRQEkdrar 633
Cdd:PRK02224 459 qpvEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAED--RIERLEERREDLEELIAERRET----- 531
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 176866331 634 edaarerARDREERLAALsaaqQEAMEELQKKIQMKHDESSRRHmEQMEQRKEKAAELSSGRHANTD 700
Cdd:PRK02224 532 -------IEEKRERAEEL----RERAAELEAEAEEKREAAAEAE-EEAEEAREEVAELNSKLAELKE 586
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
258-628 |
2.15e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 42.44 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 258 YIPAEKPAKKDAEG--WETVQRGRSMRPRakvSPVLVHASPKDDSDKENQHVQPSPQDKSQdVREQEPPIPQEPSKEMEK 335
Cdd:pfam09731 39 YIPYGEEVVLYALGedPPLAPKPKTFRPL---QPSVVSAVTGESKEPKEEKKQVKIPRQSG-VSSEVAEEEKEATKDAAE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 336 TPVIEPQSMAEVLAKKEEMADRLEKANEEAIASAIAEEEQLTREIQAENSELEtdnesdfsasigsgscglNLDWSEMLA 415
Cdd:pfam09731 115 AKAQLPKSEQEKEKALEEVLKEAISKAESATAVAKEAKDDAIQAVKAHTDSLK------------------EASDTAEIS 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 416 DYEAREPWRQstswgdiVEEEPARppghgihmheklsspsRKRTIAESKKKHEEKQLKAqqLRDKLREEKTHKLQKLMER 495
Cdd:pfam09731 177 REKATDSALQ-------KAEALAE----------------KLKEVINLAKQSEEEAAPP--LLDAAPETPPKLPEHLDNV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 496 EKDVRKWKEELLDqrrkmmeekllhAEFKRELQLQAIVKKAQEEEAKVNEI-AFINTLEAQNKR--HDVLAK----LDEY 568
Cdd:pfam09731 232 EEKVEKAQSLAKL------------VDQYKELVASERIVFQQELVSIFPDIiPVLKEDNLLSNDdlNSLIAHahreIDQL 299
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 176866331 569 EQRLNELQEERQRRQEE--KQARDEAVQERKRVLEAERQARVEELLMKRREQEARIEQQRQE 628
Cdd:pfam09731 300 SKKLAELKKREEKHIERalEKQKEELDKLAEELSARLEEVRAADEAQLRLEFEREREEIRES 361
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
449-629 |
2.21e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 449 EKLSSPSRKRTIAESKKKHEEKQLKaqQLRDKLrEEKTHKLQKLMEREKDV-------------RKWKEELLDQRRKMme 515
Cdd:PRK03918 238 EEIEELEKELESLEGSKRKLEEKIR--ELEERI-EELKKEIEELEEKVKELkelkekaeeyiklSEFYEEYLDELREI-- 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 516 EKLLhAEFKRELQ-LQAIVKKAQEEEAKVNEIAfiNTLEAQNKRhdvLAKLDEYEQRLNELQEERQRRQEEKQAR-DEAV 593
Cdd:PRK03918 313 EKRL-SRLEEEINgIEERIKELEEKEERLEELK--KKLKELEKR---LEELEERHELYEEAKAKKEELERLKKRLtGLTP 386
|
170 180 190
....*....|....*....|....*....|....*.
gi 176866331 594 QERKRVLEAERQARvEELLMKRREQEARIEQQRQEK 629
Cdd:PRK03918 387 EKLEKELEELEKAK-EEIEEEISKITARIGELKKEI 421
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
460-690 |
2.34e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.43 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 460 IAESKKKHEEKQLKAQQLRDKLREEKThKLQKLMEREKDVRKWKEELLDQRRKMMEEKLLHAEFKRelqlqaIVKKAQEE 539
Cdd:COG1340 73 VKELKEERDELNEKLNELREELDELRK-ELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKE------LVEKIKEL 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 540 EAKVNEIAFIntLEAQNKRHDVLAKLDEYEQRLNELQEERQRRQEEKQARDEAVQERKRVLEAERqARVEELLMKRREQE 619
Cdd:COG1340 146 EKELEKAKKA--LEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELR-KEADELHKEIVEAQ 222
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 176866331 620 ARIEQQRQEkdraredaarerardreerLAALSAAQQEAMEELQKKIQMKHDESSRRHMEQMEQRKEKAAE 690
Cdd:COG1340 223 EKADELHEE-------------------IIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAEEIFE 274
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
586-713 |
2.67e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 41.86 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 586 KQARDEAVQER--KRVLEAERqarveellmKRREQEA--RIEQQRQEKDRAREdaarerardreerlAALSAAQQEAMEE 661
Cdd:pfam15709 332 KASRDRLRAERaeMRRLEVER---------KRREQEEqrRLQQEQLERAEKMR--------------EELELEQQRRFEE 388
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 176866331 662 LQKKIQMKHDESSRRHMEQMEQRKEKAAELSSGRHANTDYAPKLTPYERKKQ 713
Cdd:pfam15709 389 IRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQ 440
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
449-629 |
3.18e-03 |
|
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: 41.29 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 449 EKLSSPSRKRTIAESKKKHEEKQLKAQQLRDKLREEKTHKLQK-LMEREKDVRKWKEELLDQRRKMMEEKLLHAEFKREL 527
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQeLAALEAELAELEKEIAELRAELEAQKEELAELLRAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 528 Q-------LQAIVKKAQEEEAKVNEIAFINTLEAQNKRhdvLAKLDEYEQRLNELQEERQRRQEEKQARDEAVQERKRVL 600
Cdd:COG4942 114 YrlgrqppLALLLSPEDFLDAVRRLQYLKYLAPARREQ---AEELRADLAELAALRAELEAERAELEALLAELEEERAAL 190
|
170 180
....*....|....*....|....*....
gi 176866331 601 EAERQARvEELLMKRREQEARIEQQRQEK 629
Cdd:COG4942 191 EALKAER-QKLLARLEKELAELAAELAEL 218
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
342-601 |
4.23e-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: 41.59 E-value: 4.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 342 QSMAEVLAKKEEMADRLEKANEEA-------IASAIAEEEQLTREIQAENSELEtdnesDFSASIGSGSCGLNLDWSEML 414
Cdd:TIGR02169 265 KRLEEIEQLLEELNKKIKDLGEEEqlrvkekIGELEAEIASLERSIAEKERELE-----DAEERLAKLEAEIDKLLAEIE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 415 ADYEAREPWR-QSTSWGDIVEEeparppghgihmheklsspsRKRTIAESKKKHEEKQLKAQQLRDKLREEKThKLQKLM 493
Cdd:TIGR02169 340 ELEREIEEERkRRDKLTEEYAE--------------------LKEELEDLRAELEEVDKEFAETRDELKDYRE-KLEKLK 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 494 EREKDVRKWKEELLDQRRKMMEEKL-LHAEFKR----ELQLQAIVKKAQEE----EAKVNEIAFIntLEAQNKRH-DVLA 563
Cdd:TIGR02169 399 REINELKRELDRLQEELQRLSEELAdLNAAIAGieakINELEEEKEDKALEikkqEWKLEQLAAD--LSKYEQELyDLKE 476
|
250 260 270
....*....|....*....|....*....|....*...
gi 176866331 564 KLDEYEQRLNELQEERQRRQEEKQARDEAVQERKRVLE 601
Cdd:TIGR02169 477 EYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEE 514
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
457-625 |
4.61e-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: 4.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 457 KRTIAESKKKHEEKQLKAQQLRDKL---REEKTHKLQKLMEREKDVRKWKEELLDQRRKMMEEKLLHAEFKREL--QLQA 531
Cdd:COG4913 698 EAELEELEEELDELKGEIGRLEKELeqaEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLeeRIDA 777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 532 IVKKAQEEEAKVNEI--AFINTLEAQNKRHDV-LAKLDEYEQRLNELqeerqrrqeekQARD--EAVQERKRVLEAERQA 606
Cdd:COG4913 778 LRARLNRAEEELERAmrAFNREWPAETADLDAdLESLPEYLALLDRL-----------EEDGlpEYEERFKELLNENSIE 846
|
170
....*....|....*....
gi 176866331 607 RVEELLMKRREQEARIEQQ 625
Cdd:COG4913 847 FVADLLSKLRRAIREIKER 865
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
464-692 |
4.66e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.49 E-value: 4.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 464 KKKHEEKQLKAQQLRDKLREEKTHKLQKLMEREKDVRKWKEELLDQRRKMMEEKLLHAEFKRELQLQAIVKKAQEEEAKV 543
Cdd:TIGR00618 657 QERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAA 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 544 NEIAFINTL-EAQNKRHDVLAKLDEYEQRLNElqeerqrRQEEKQARDEAVQERKRVLEAERQARvEELLMKRREQEARI 622
Cdd:TIGR00618 737 REDALNQSLkELMHQARTVLKARTEAHFNNNE-------EVTAALQTGAELSHLAAEIQFFNRLR-EEDTHLLKTLEAEI 808
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 623 EQQRQEKDRAREDAARERARDREERLAALSAAQQEAMEELQkkiQMKHDESSRRHMEQMEQRKEKAAELS 692
Cdd:TIGR00618 809 GQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITH---QLLKYEECSKQLAQLTQEQAKIIQLS 875
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
457-668 |
4.98e-03 |
|
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: 40.67 E-value: 4.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 457 KRTIAESKKKHEEKQLKAQQLRDKLRE---EKTHKLQKLMEREKDVRKWKEELLDQRRKMMEEKLLHAEFKRELQLQAIV 533
Cdd:pfam13868 133 DEFNEEQAEWKELEKEEEREEDERILEylkEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQ 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 534 KkAQEEEAKVNEIAfintlEAQNKRHDVLAKLDEYEQRLNELQEERQRRQEEKQARDEAVQERKRVLEAERQARVEELLM 613
Cdd:pfam13868 213 E-EQERKERQKERE-----EAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRM 286
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 176866331 614 KRREQEARIEQQRQEKDRAREDAARERARDREERLAALSAAQQEAMEELQKKIQM 668
Cdd:pfam13868 287 KRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKKLKE 341
|
|
| eIF3_subunit |
pfam08597 |
Translation initiation factor eIF3 subunit; This is a family of proteins which are subunits of ... |
298-393 |
5.17e-03 |
|
Translation initiation factor eIF3 subunit; This is a family of proteins which are subunits of the eukaryotic translation initiation factor 3 (eIF3). In yeast it is called Hcr1. The Saccharomyces cerevisiae protein Swiss:Q05775 has been shown to be required for processing of 20S pre-rRNA and binds to 18S rRNA and eIF3 subunits Rpg1p and Prt1p.
Pssm-ID: 462530 Cd Length: 239 Bit Score: 39.97 E-value: 5.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 298 DDSDKENQHVQPSPQDKSQ--------------DVREQEPPIPQEPSKEMEKTPVIEPQSMAEVLAKKEEMADRLEKANE 363
Cdd:pfam08597 5 DDEDFEPSSPAPPPARRDKwddedededvkdswDAEEEEEEEKEKAAKAAAAKAKKKKKSKKQKIAEKEAERKAEEEAEE 84
|
90 100 110
....*....|....*....|....*....|
gi 176866331 364 EAiasAIAEEEQLTREIQAENSELETDNES 393
Cdd:pfam08597 85 EE---ELTPEDEAARKLRLRKAEEESDLEN 111
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
459-628 |
7.40e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.27 E-value: 7.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 459 TIAESKKKHEEKQLKAQQLRDKLREEKTHKLQKLMEREKDVRKWKEELLDQRRKMME-EKLLHAEFKRELQLQAIVKKAQ 537
Cdd:COG4372 28 ALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEElNEQLQAAQAELAQAQEELESLQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 538 EEEAKVNEIafINTLEAQNKrhdvlaKLDEYEQRLNELQEERQRRQEEKQARDEAVQERKRVLEAE-RQARVEELLMKRR 616
Cdd:COG4372 108 EEAEELQEE--LEELQKERQ------DLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEElAALEQELQALSEA 179
|
170
....*....|..
gi 176866331 617 EQEARIEQQRQE 628
Cdd:COG4372 180 EAEQALDELLKE 191
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
342-693 |
8.02e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 8.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 342 QSMAEVLAKKEEMADRLEK-ANEEAIASAIAEEEQLTREIQAENSELEtdnesDFSASIgsgscglnLDWSEMLADYEAR 420
Cdd:COG4717 102 EELEELEAELEELREELEKlEKLLQLLPLYQELEALEAELAELPERLE-----ELEERL--------EELRELEEELEEL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 421 EpwRQSTSWGDIVEEEPARPPghgIHMHEKLSSPSRKRTIAESKKKHEEKQLKAQQLRDKLREEKTHKLQKLMEREKDVR 500
Cdd:COG4717 169 E--AELAELQEELEELLEQLS---LATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 501 KWKEE-------------------------------------LLDQRRKMMEEKLLHAEFKRELQLQAIVKKAQEEE--- 540
Cdd:COG4717 244 RLKEArlllliaaallallglggsllsliltiagvlflvlglLALLFLLLAREKASLGKEAEELQALPALEELEEEElee 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 541 --------AKVNEIAFINTLEAQNKRHDVLAKLDEYEQRL--NELQEERQRRQEEKQARDEAVQERKrvleAERQARVEE 610
Cdd:COG4717 324 llaalglpPDLSPEELLELLDRIEELQELLREAEELEEELqlEELEQEIAALLAEAGVEDEEELRAA----LEQAEEYQE 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 176866331 611 LLMKRREQEARIEQQRQEKDRAREDAARERARDREERLAALSAAQQEAMEELQKKI-----QMKHDESSRRHMEQMEQRK 685
Cdd:COG4717 400 LKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELaeleaELEQLEEDGELAELLQELE 479
|
....*...
gi 176866331 686 EKAAELSS 693
Cdd:COG4717 480 ELKAELRE 487
|
|
| |
