|
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 ... |
89-186 |
5.35e-56 |
|
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: 188.77 E-value: 5.35e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 89 KTRHPRKIDLRARYWAFLFDNLRRAVDEIYVTCESDQSVVECKEVLMMLDNYVRDFKALIDWIQLQEKLEKTDAQSRPTS 168
Cdd:pfam16501 1 STGRDKKSELRARYWAFLFDNLQRAVDEIYQTCESDESVVECKEVIMVLDNYTRDFKALIEWFRLKWDYENTPPPQRPTS 80
|
90
....*....|....*...
gi 225579092 169 LAWEVKKMSPGRHVIPSP 186
Cdd:pfam16501 81 LAWEVRKSSPGKSVNKSP 98
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
537-771 |
3.03e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.51 E-value: 3.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 537 KRTIAESKKKHEEKQMKAQQLREKLREEkTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQLQAIVKKA 616
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEEL-ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 617 QEEEAKVNEIAFINTL-EAQNKRHDVLSKLKEYEQRLNELqeerqrRQEEKQARDEAVQERKRALEAERQARVEELLMKR 695
Cdd:COG1196 331 ELEELEEELEELEEELeEAEEELEEAEAELAEAEEALLEA------EAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 225579092 696 KEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQkKIQLKHDESIRRHMEQIEQRKEKAAEL 771
Cdd:COG1196 405 LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA-ELEEEEEALLELLAELLEEAALLEAAL 479
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
392-770 |
5.72e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 70.94 E-value: 5.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 392 QVNEEKFPAEKARIENEMDPSDISNSMAEVLAKKEELADRLEKANEEAIASAIAEEEQLTREiEAEENNDinietdndsd 471
Cdd:PTZ00121 1432 KADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAE-EAKKKAD---------- 1500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 472 fsasmgsgsvsfcgmsmdwndvladyEARESWRQNTSWGDIVEEEPARPPGHGIHMHEKLSSPSRKRtiAESKKKHEEKQ 551
Cdd:PTZ00121 1501 --------------------------EAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKK--AEEKKKADELK 1552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 552 mKAQQLReKLREEKTLKLQKLLEREKDVRKWKEELLDQ--RRRMMEEKLLHAEFKREVQLQAivKKAQEEEAKVNEIafi 629
Cdd:PTZ00121 1553 -KAEELK-KAEEKKKAEEAKKAEEDKNMALRKAEEAKKaeEARIEEVMKLYEEEKKMKAEEA--KKAEEAKIKAEEL--- 1625
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 630 NTLEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARD--EAVQERKRALE---AERQARVEELLMKRKEQEARIEQ 704
Cdd:PTZ00121 1626 KKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEakKAEEDKKKAEEakkAEEDEKKAAEALKKEAEEAKKAE 1705
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 225579092 705 QRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIRRHMEQIEQRKEKAAE 770
Cdd:PTZ00121 1706 ELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAE 1771
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
549-770 |
3.06e-11 |
|
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: 3.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 549 EKQMKAQQLREKLRE-EKTLKLQKLLEREKDVRKWKEELLDQRRRmmEEKLLHAEFKREVQLQAIVKKAQEEEAKVNEia 627
Cdd:COG1196 210 EKAERYRELKEELKElEAELLLLKLRELEAELEELEAELEELEAE--LEELEAELAELEAELEELRLELEELELELEE-- 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 628 fintleAQNKRHDVLSKLKEYEQRLNELQeerQRRQEEKQARDEAVQERKRALE--AERQARVEELLMKRKEQEARIEQQ 705
Cdd:COG1196 286 ------AQAEEYELLAELARLEQDIARLE---ERRRELEERLEELEEELAELEEelEELEEELEELEEELEEAEEELEEA 356
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 225579092 706 RQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIRRHMEQIEQRKEKAAE 770
Cdd:COG1196 357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
345-711 |
9.90e-11 |
|
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: 66.63 E-value: 9.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 345 QFTVSTLDD--VKNSGSIRDNYVRTSEISAVHIDTECVSVMLQAGTPPLQVNEEKFPAEKARIENEMDP-----SDISNS 417
Cdd:TIGR02169 638 KYRMVTLEGelFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDElsqelSDASRK 717
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 418 MAEVLAKKEELADRLEKANEEaiasaIAEEEQLTREIEAEENNDINIETDNDSDFSAsmgsgsvsfcgMSMDWNDV---L 494
Cdd:TIGR02169 718 IGEIEKEIEQLEQEEEKLKER-----LEELEEDLSSLEQEIENVKSELKELEARIEE-----------LEEDLHKLeeaL 781
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 495 ADYEARES---WRQNTSWGDIVEEEPARPPGHGIHMHEKLSSPSRKRTIAESKKKHEEKQMKAQQLREKLREEK----TL 567
Cdd:TIGR02169 782 NDLEARLShsrIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEienlNG 861
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 568 KLQKLLEREKDVRKWKEELLDQRRRMMEEKLlhaefKREVQLQAIVKKAQEEEAKVnEIAFINTLEAQNKRHDVLSKLKE 647
Cdd:TIGR02169 862 KKEELEEELEELEAALRDLESRLGDLKKERD-----ELEAQLRELERKIEELEAQI-EKKRKRLSELKAKLEALEEELSE 935
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 648 YEQRLNELQEERQRRQEEK--QARDEAVQERKRALE----------AERQARVEELLMK-------RKEQEARIEQQRQE 708
Cdd:TIGR02169 936 IEDPKGEDEEIPEEELSLEdvQAELQRVEEEIRALEpvnmlaiqeyEEVLKRLDELKEKrakleeeRKAILERIEEYEKK 1015
|
...
gi 225579092 709 KEK 711
Cdd:TIGR02169 1016 KRE 1018
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
537-929 |
1.80e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.93 E-value: 1.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 537 KRTIAESKKKHEEKQmKAQQLREKLREEKtlKLQKLLEREKDVRKWKEEL---------LDQRRRMMEEKLLHAEFKREV 607
Cdd:PTZ00121 1456 AKKAEEAKKKAEEAK-KADEAKKKAEEAK--KADEAKKKAEEAKKKADEAkkaaeakkkADEAKKAEEAKKADEAKKAEE 1532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 608 QLQAIVKKAQEEEAKVNEIAFINTLEAQNKRHDVLSKLKEYEQRLNELqeerQRRQEEKQARDEAVQERKRALEAERQAR 687
Cdd:PTZ00121 1533 AKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMAL----RKAEEAKKAEEARIEEVMKLYEEEKKMK 1608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 688 VEELlmkRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDEsirrhmeqiEQRKEK 767
Cdd:PTZ00121 1609 AEEA---KKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKA---------EEDKKK 1676
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 768 AAELSSGRHANTDYAPKLTPYERKKQcslcnvlISSEVYLFSHVKGRKHQQAVR--ENTSIQGRELSDEEVEhlslkkyi 845
Cdd:PTZ00121 1677 AEEAKKAEEDEKKAAEALKKEAEEAK-------KAEELKKKEAEEKKKAEELKKaeEENKIKAEEAKKEAEE-------- 1741
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 846 idivvESTAPAEALKDGEERQKNKKKAKKIKARMNFRAKEYESLMETKNSGSDSPYKAKLQRLAKDLLKQVQVQDSGSWA 925
Cdd:PTZ00121 1742 -----DKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKE 1816
|
....
gi 225579092 926 NNKV 929
Cdd:PTZ00121 1817 GNLV 1820
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
423-767 |
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 225579092 423 AKKEELADRLEK---ANEEAIASAIAEEEQLTREIEA--EENNDINIETDNDSDFSASMGSgsvsfcgmsmDWNDVLADY 497
Cdd:PRK02224 359 EELREEAAELESeleEAREAVEDRREEIEELEEEIEElrERFGDAPVDLGNAEDFLEELRE----------ERDELRERE 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 498 EARESWRQNTSwGDIVEEEPARPPGHGIHMHEKLSSPSRKRTIAESKKKHEEKQMKAQQLREKL--------REEKTLKL 569
Cdd:PRK02224 429 AELEATLRTAR-ERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVeeveerleRAEDLVEA 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 570 QKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKR----------EVQLQAIVKKAQEEEAKVNEIAFIN--------T 631
Cdd:PRK02224 508 EDRIERLEERREDLEELIAERRETIEEKRERAEELReraaeleaeaEEKREAAAEAEEEAEEAREEVAELNsklaelkeR 587
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 632 LEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQ---ERKRALEAERQ-ARVEELLMKRKEQEARIEQQRQ 707
Cdd:PRK02224 588 IESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAekrERKRELEAEFDeARIEEAREDKERAEEYLEQVEE 667
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 225579092 708 EkekaredaarerardreerLAALTaaqqEAMEELQKKI-----QLKHDESIRRHMEQIEQRKEK 767
Cdd:PRK02224 668 K-------------------LDELR----EERDDLQAEIgavenELEELEELRERREALENRVEA 709
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
536-770 |
4.47e-10 |
|
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: 63.01 E-value: 4.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 536 RKRTIAESKKKHEEKQMKAQQLREKLREEKtLKLQKLLEREKDvrkwkEELLDQRRRMMEEKLLHAEFKREVQLQAIVKK 615
Cdd:pfam13868 71 RKRYRQELEEQIEEREQKRQEEYEEKLQER-EQMDEIVERIQE-----EDQAEAEEKLEKQRQLREEIDEFNEEQAEWKE 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 616 AQEEEAKVNE---IAFINTLEAQNKRHDVLSKLKEY--EQRLNELQEERQRRQEEKQARDEAVQER-KRALEAERQARVE 689
Cdd:pfam13868 145 LEKEEEREEDeriLEYLKEKAEREEEREAEREEIEEekEREIARLRAQQEKAQDEKAERDELRAKLyQEEQERKERQKER 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 690 ELLMKRKEQEARI----EQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKK--IQLKHDESIRRHMEQIEQ 763
Cdd:pfam13868 225 EEAEKKARQRQELqqarEEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRrmKRLEHRRELEKQIEEREE 304
|
....*..
gi 225579092 764 RKEKAAE 770
Cdd:pfam13868 305 QRAAERE 311
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
530-710 |
8.28e-10 |
|
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: 63.60 E-value: 8.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 530 KLSSPSRKRTIAESKKKHEEKQMKAQQLRE----KLREEKTLKLQKL----LEREKDVRKWKEELLDQRRRMMEeklLHA 601
Cdd:pfam17380 405 KILEEERQRKIQQQKVEMEQIRAEQEEARQrevrRLEEERAREMERVrleeQERQQQVERLRQQEEERKRKKLE---LEK 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 602 EFKREVQLQAIVKKAQEEEAKVNEIAFIntlEAQNKRHDVLsklKEYEQRLNELQEerqrrqeeKQARDEAVQERKRALE 681
Cdd:pfam17380 482 EKRDRKRAEEQRRKILEKELEERKQAMI---EEERKRKLLE---KEMEERQKAIYE--------EERRREAEEERRKQQE 547
|
170 180
....*....|....*....|....*....
gi 225579092 682 AERQARVEELLMKRKEQEARIEQQRQEKE 710
Cdd:pfam17380 548 MEERRRIQEQMRKATEERSRLEAMERERE 576
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
535-864 |
1.35e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.24 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 535 SRKRTIAESKKKHEEKQmKAQQLREKLREEKtlKLQKLLEREKDVRKWKEELldqrRRMMEEKLLHAEFKR---EVQLQA 611
Cdd:PTZ00121 1362 AEEKAEAAEKKKEEAKK-KADAAKKKAEEKK--KADEAKKKAEEDKKKADEL----KKAAAAKKKADEAKKkaeEKKKAD 1434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 612 IVKKAQEEEAKVNEIafiNTLEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQArvEEl 691
Cdd:PTZ00121 1435 EAKKKAEEAKKADEA---KKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAA--EA- 1508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 692 lmKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIRRHMEQIEQRKEKAAEL 771
Cdd:PTZ00121 1509 --KKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEA 1586
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 772 SSGRHANTDYAPKLTPYERKKQCSlcnvlissevylfshvKGRKHQQAVRENTSIQGRELSDEEVEHLSLKKyiidivVE 851
Cdd:PTZ00121 1587 KKAEEARIEEVMKLYEEEKKMKAE----------------EAKKAEEAKIKAEELKKAEEEKKKVEQLKKKE------AE 1644
|
330
....*....|...
gi 225579092 852 STAPAEALKDGEE 864
Cdd:PTZ00121 1645 EKKKAEELKKAEE 1657
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
540-772 |
2.50e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.88 E-value: 2.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 540 IAESKKKHEEKQMKAQQLREKLRE------EKTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQLQAIV 613
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYEllaelaRLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 614 KKAQEEEAKVNEIAFINTL-EAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQARvEELL 692
Cdd:COG1196 349 AEEELEEAEAELAEAEEALlEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEEL-EELE 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 693 MKRKEQEARIEQQRQEKEKaredaarerARDREERLAALTAAQQEAMEELQKKIQLKHDESIRRHMEQIEQRKEKAAELS 772
Cdd:COG1196 428 EALAELEEEEEEEEEALEE---------AAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
535-764 |
2.67e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.88 E-value: 2.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 535 SRKRTIAESKKKHEEKQMKAQQLREKLREEKTLKLQKLLEREKDVRKWKEEL--LDQRRRMMEEKLLHAEFKREVQLQAI 612
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELeeAEEELEEAEAELAEAEEALLEAEAEL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 613 VKKAQEEEAKVNEIAfiNTLEAQNKRHDVLSKLKEYEQRLNELqeeRQRRQEEKQARDEAVQERKRALEAERQARVEELL 692
Cdd:COG1196 375 AEAEEELEELAEELL--EALRAAAELAAQLEELEEAEEALLER---LERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 225579092 693 MKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIRRHMEQIEQR 764
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRG 521
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
537-770 |
2.02e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.92 E-value: 2.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 537 KRTIAESKKKHEEKQMKAQQLREKLRE---EKTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEF-KREVQLQAI 612
Cdd:PRK03918 171 IKEIKRRIERLEKFIKRTENIEELIKEkekELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIeELEKELESL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 613 VKKAQEEEAKVNEI-AFINTLEAQnkrhdvLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQE------RKRALEAERQ 685
Cdd:PRK03918 251 EGSKRKLEEKIRELeERIEELKKE------IEELEEKVKELKELKEKAEEYIKLSEFYEEYLDElreiekRLSRLEEEIN 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 686 ArVEELLMKRKEQEARIEQQRQEKEKAREDAARERARDREERLAaltAAQQEAMEELQKKIQLKHDESIRRHMEQIEQRK 765
Cdd:PRK03918 325 G-IEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEA---KAKKEELERLKKRLTGLTPEKLEKELEELEKAK 400
|
....*
gi 225579092 766 EKAAE 770
Cdd:PRK03918 401 EEIEE 405
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
529-771 |
2.11e-08 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 58.34 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 529 EKLSSPSRKRTIAESKKKHEEKQMKAQQLREKLREEKTLKLqkllEREKDVRKWKEELLDQRRRMMEEKLLHAEFKrEVQ 608
Cdd:pfam02029 96 EKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIR----EKEYQENKWSTEVRQAEEEGEEEEDKSEEAE-EVP 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 609 LQAIVKKAQEEEAKVNEIAFINTLEA--QNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERqa 686
Cdd:pfam02029 171 TENFAKEEVKDEKIKKEKKVKYESKVflDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQ-- 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 687 RVEELLMKRKEQEAR-IEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKkiQLKHDESIRRHMEQIEQRK 765
Cdd:pfam02029 249 KLEELRRRRQEKESEeFEKLRQKQQEAELELEELKKKREERRKLLEEEEQRRKQEEAER--KLREEEEKRRMKEEIERRR 326
|
....*.
gi 225579092 766 EKAAEL 771
Cdd:pfam02029 327 AEAAEK 332
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
536-770 |
2.90e-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: 57.24 E-value: 2.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 536 RKRTIAESKK----KHEEKQMKAQQLREKLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLL-HAEFKRE-VQL 609
Cdd:pfam13868 24 RDAQIAEKKRikaeEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEeYEEKLQErEQM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 610 QAIVKKAQEEEAKVNEIAFI---NTLEAQNKRHDVLSKLKEYE-QRLNELQEERQRRQEEKQARDEAVQERKRALEAERQ 685
Cdd:pfam13868 104 DEIVERIQEEDQAEAEEKLEkqrQLREEIDEFNEEQAEWKELEkEEEREEDERILEYLKEKAEREEEREAEREEIEEEKE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 686 ARVEELLmkrkEQEARIEQQRQEKEKaredaarerardreeRLAALTAAQQEA------MEELQKKIQLKHD--ESIRRH 757
Cdd:pfam13868 184 REIARLR----AQQEKAQDEKAERDE---------------LRAKLYQEEQERkerqkeREEAEKKARQRQElqQAREEQ 244
|
250
....*....|...
gi 225579092 758 MEQIEQRKEKAAE 770
Cdd:pfam13868 245 IELKERRLAEEAE 257
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
542-770 |
3.58e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.53 E-value: 3.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 542 ESKKKHEEKQM-KAQQLREKLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQ--LQAIVKKAQE 618
Cdd:TIGR02168 199 ERQLKSLERQAeKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEekLEELRLEVSE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 619 EEAKVNEI--------AFINTLEAQ-----NKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERq 685
Cdd:TIGR02168 279 LEEEIEELqkelyalaNEISRLEQQkqilrERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLE- 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 686 ARVEELLMKRKEQEARIEQQRQEKEKaredaarerardreerLAALTAAQQEAMEELQKKIQlkhdeSIRRHMEQIEQRK 765
Cdd:TIGR02168 358 AELEELEAELEELESRLEELEEQLET----------------LRSKVAQLELQIASLNNEIE-----RLEARLERLEDRR 416
|
....*
gi 225579092 766 EKAAE 770
Cdd:TIGR02168 417 ERLQQ 421
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
542-770 |
4.57e-08 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 58.06 E-value: 4.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 542 ESKKKHEEKQMKAQQLREKLREEKTLKlqKLLEREKD-----VRKWKEELLDQRRRMMEEKLLHAEFKREVQ-------- 608
Cdd:pfam02463 174 ALKKLIEETENLAELIIDLEELKLQEL--KLKEQAKKaleyyQLKEKLELEEEYLLYLDYLKLNEERIDLLQellrdeqe 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 609 ----LQAIVKKAQEEEAKVNEIAFINT--LEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEA 682
Cdd:pfam02463 252 eiesSKQEIEKEEEKLAQVLKENKEEEkeKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 683 ERQARVEELLMKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQ--EAMEELQKKIQLKH-DESIRRHME 759
Cdd:pfam02463 332 KEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERlsSAAKLKEEELELKSeEEKEAQLLL 411
|
250
....*....|.
gi 225579092 760 QIEQRKEKAAE 770
Cdd:pfam02463 412 ELARQLEDLLK 422
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
542-770 |
1.15e-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: 56.29 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 542 ESKKKHEEKQMKAQQL--REKLREEKTLKlQKLLEREKDVRKWKEELLDQRRRMMEeKLLHAEFKREVQlqaivKKAQEE 619
Cdd:pfam17380 297 EQERLRQEKEEKAREVerRRKLEEAEKAR-QAEMDRQAAIYAEQERMAMERERELE-RIRQEERKRELE-----RIRQEE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 620 EA----KVNEIAFINtLEAQNKRHDVLSKLK-------EYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQ--- 685
Cdd:pfam17380 370 IAmeisRMRELERLQ-MERQQKNERVRQELEaarkvkiLEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERArem 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 686 ARVEELLMKRKEQEARIEQQRQE-------KEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIRRHM 758
Cdd:pfam17380 449 ERVRLEEQERQQQVERLRQQEEErkrkkleLEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKA 528
|
250
....*....|..
gi 225579092 759 EQIEQRKEKAAE 770
Cdd:pfam17380 529 IYEEERRREAEE 540
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
535-770 |
1.32e-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: 56.60 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 535 SRKRTIAESKKKHEEKQMKAQQLREKLREektlKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQ------ 608
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAE----LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEqleeri 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 609 --LQAIVKKAQEEEAKVNEiafiNTLEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALeAERQA 686
Cdd:TIGR02168 750 aqLSKELTELEAEIEELEE----RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA-ANLRE 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 687 RVEELLMKRKEQEARIEQQRQEKEKaredaarerARDREERLAALTAAQQEAMEELQKKIQLKHDE--SIRRHMEQIEQR 764
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEEQIEE---------LSEDIESLAAEIEELEELIEELESELEALLNEraSLEEALALLRSE 895
|
....*.
gi 225579092 765 KEKAAE 770
Cdd:TIGR02168 896 LEELSE 901
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
537-780 |
3.22e-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: 55.07 E-value: 3.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 537 KRTIAESK---KKHEEKQMKAQQLREKLREEKTlKLQKLLEREK-DVRKWKEELLDQRRRMMEekllhaefkrevqlqaI 612
Cdd:TIGR02169 307 ERSIAEKErelEDAEERLAKLEAEIDKLLAEIE-ELEREIEEERkRRDKLTEEYAELKEELED----------------L 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 613 VKKAQEEEAKVNEiafinTLEAQNKRHDVLSKLKEyeqRLNELQEERQRRQEEKQARDEAVQERKRALE------AERQA 686
Cdd:TIGR02169 370 RAELEEVDKEFAE-----TRDELKDYREKLEKLKR---EINELKRELDRLQEELQRLSEELADLNAAIAgieakiNELEE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 687 RVEELLMKRKEQEARIEQQRQEKEKaredaarerardREERLAALTAAQQEAMEELQKKiqlkhdesiRRHMEQIEQRKE 766
Cdd:TIGR02169 442 EKEDKALEIKKQEWKLEQLAADLSK------------YEQELYDLKEEYDRVEKELSKL---------QRELAEAEAQAR 500
|
250
....*....|....
gi 225579092 767 KAAELSSGRHANTD 780
Cdd:TIGR02169 501 ASEERVRGGRAVEE 514
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
539-917 |
3.84e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.15 E-value: 3.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 539 TIAESKKKHEEKQMKaqqlrEKLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMMEEkllhAEFKREVQLQAIVKKAqe 618
Cdd:PTZ00121 1092 ATEEAFGKAEEAKKT-----ETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEE----ARKAEDAKRVEIARKA-- 1160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 619 EEAKVNEIAfintLEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQARVEELL----MK 694
Cdd:PTZ00121 1161 EDARKAEEA----RKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKkaeeAK 1236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 695 RKEQEA-RIEQQRQEKEKAREDAARERARDREErlAALTAAQQEAMEELQKKIQLKHDESIRRHME--QIEQRKEKAAEL 771
Cdd:PTZ00121 1237 KDAEEAkKAEEERNNEEIRKFEEARMAHFARRQ--AAIKAEEARKADELKKAEEKKKADEAKKAEEkkKADEAKKKAEEA 1314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 772 SSGRHA--NTDYAPKLTPYERKKqcslcnvliSSEVYLFSHVKGRKHQQAVREntsiqgRELSDEEVEHLSLKKYiidiv 849
Cdd:PTZ00121 1315 KKADEAkkKAEEAKKKADAAKKK---------AEEAKKAAEAAKAEAEAAADE------AEAAEEKAEAAEKKKE----- 1374
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 225579092 850 vESTAPAEALKDGEERQKNKKKAKKIKARMNFRAKEYESLMETKNSGSDSPYKAKLQRLAKDLLKQVQ 917
Cdd:PTZ00121 1375 -EAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAE 1441
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
509-764 |
4.81e-07 |
|
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: 53.70 E-value: 4.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 509 WGDIVEEEPARPPGHGIHMHEKLSSPSRKRTIAESKKKHEEKQMKAQQLREK--LREEKTLKLQKLLErEKDVRKWKEEL 586
Cdd:TIGR02794 20 LGSLYHSVKPEPGGGAEIIQAVLVDPGAVAQQANRIQQQKKPAAKKEQERQKklEQQAEEAEKQRAAE-QARQKELEQRA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 587 LDQRRRMMEEKllHAEFKREVQLQAIVKKA-QEEEAKVNEiafintlEAQNKRhdvlsKLKEYEQRLNELQEERQRRQEE 665
Cdd:TIGR02794 99 AAEKAAKQAEQ--AAKQAEEKQKQAEEAKAkQAAEAKAKA-------EAEAER-----KAKEEAAKQAEEEAKAKAAAEA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 666 KQARDEAV----QERKRALEAERQARVEELLMKRKEQEARIEQQRQEK---EKAREDAARERARDREERLAALTAAQQEA 738
Cdd:TIGR02794 165 KKKAEEAKkkaeAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKaeaEAAAAAAAEAERKADEAELGDIFGLASGS 244
|
250 260
....*....|....*....|....*..
gi 225579092 739 MEELQKKIQLKHDES-IRRHMEQIEQR 764
Cdd:TIGR02794 245 NAEKQGGARGAAAGSeVDKYAAIIQQA 271
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
538-770 |
5.25e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 54.01 E-value: 5.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 538 RTIAESKKKHEEKQMKaQQLREKLREEKTLKLQKLLErekdvrkWKEELLDQRRrmmeekllhaEFKREVqlqaivkKAQ 617
Cdd:PRK12704 26 KKIAEAKIKEAEEEAK-RILEEAKKEAEAIKKEALLE-------AKEEIHKLRN----------EFEKEL-------RER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 618 EEEakvneiafintLEAQNKRhdvlskLKEYEQRLNElqeerqrrqeekqaRDEAVQERKRALEAERQ---ARVEELLMK 694
Cdd:PRK12704 81 RNE-----------LQKLEKR------LLQKEENLDR--------------KLELLEKREEELEKKEKeleQKQQELEKK 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 225579092 695 RKEQEARIEQQRQEKEKaredaarerardreerLAALTA--AQQEAMEELQKKIQLKHDESIRRHMEQIEQRKEKAAE 770
Cdd:PRK12704 130 EEELEELIEEQLQELER----------------ISGLTAeeAKEILLEKVEEEARHEAAVLIKEIEEEAKEEADKKAK 191
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
540-789 |
7.08e-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: 53.97 E-value: 7.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 540 IAESKKKHEEKQMKAQQLR---EKLREEKTLKLqkllEREKDVRKWKEELLDQRRrmmeEKLLHAEFKREVQLQAIVK-- 614
Cdd:pfam17380 353 IRQEERKRELERIRQEEIAmeiSRMRELERLQM----ERQQKNERVRQELEAARK----VKILEEERQRKIQQQKVEMeq 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 615 -KAQEEEAKVNEIafiNTLEAQNKRHDVLSKLKEYE--QRLNELQEERQRRQEEKQARDEavQERKRALEAERQARVEEL 691
Cdd:pfam17380 425 iRAEQEEARQREV---RRLEEERAREMERVRLEEQErqQQVERLRQQEEERKRKKLELEK--EKRDRKRAEEQRRKILEK 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 692 LMKRKEQeARIEQQRQEK--EKAREDAARERARDREERLAALTAAQQEAMEElQKKIQ------------LKHDESIRRH 757
Cdd:pfam17380 500 ELEERKQ-AMIEEERKRKllEKEMEERQKAIYEEERRREAEEERRKQQEMEE-RRRIQeqmrkateersrLEAMEREREM 577
|
250 260 270
....*....|....*....|....*....|....*
gi 225579092 758 MEQIEQRKEKAAELSSGRHANT---DYAPKLTPYE 789
Cdd:pfam17380 578 MRQIVESEKARAEYEATTPITTikpIYRPRISEYQ 612
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
541-712 |
7.75e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 53.27 E-value: 7.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 541 AESKKKHEEKQMKAQQLREKLREEKTLKLQKLLEREKdvrkwkEELLDQrrrmmEEKLLHAEFKREVQLQAivKKAQEEE 620
Cdd:PRK09510 72 KSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEK------ERLAAQ-----EQKKQAEEAAKQAALKQ--KQAEEAA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 621 AKVNEIAFINTlEAQNKRHDVLSKLKEYEQRLNElqeerqrrqeEKQARDEAVQERKRALEAERQARVEELLMKRKEQEA 700
Cdd:PRK09510 139 AKAAAAAKAKA-EAEAKRAAAAAKKAAAEAKKKA----------EAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEA 207
|
170
....*....|..
gi 225579092 701 RIEQQRQEKEKA 712
Cdd:PRK09510 208 KKKAAAEAKKKA 219
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
551-777 |
1.32e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.02 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 551 QMKAQQLRE-----------KLREEKTLKlqKL------LEREKDVRkwkEELLDQRRR--------------MMEEKLL 599
Cdd:COG1196 151 EAKPEERRAiieeaagiskyKERKEEAER--KLeateenLERLEDIL---GELERQLEPlerqaekaeryrelKEELKEL 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 600 HAEFK----REVQLQAIVKKAQEEEAKVNEIAFINTLEAQNKRHDVL-SKLKEYEQRLNELqeerqrrqeekQARDEAVQ 674
Cdd:COG1196 226 EAELLllklRELEAELEELEAELEELEAELEELEAELAELEAELEELrLELEELELELEEA-----------QAEEYELL 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 675 ERKRALEAERQaRVEELLMKRKEQEARIEQQRQEKEKAREDAarerardrEERLAALTAAQQEAMEELQKKiQLKHDESI 754
Cdd:COG1196 295 AELARLEQDIA-RLEERRRELEERLEELEEELAELEEELEEL--------EEELEELEEELEEAEEELEEA-EAELAEAE 364
|
250 260
....*....|....*....|...
gi 225579092 755 RRHMEQIEQRKEKAAELSSGRHA 777
Cdd:COG1196 365 EALLEAEAELAEAEEELEELAEE 387
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
526-770 |
1.71e-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: 52.75 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 526 HMHEKLSSPSRKRT--IAESKKKHEEKQMKAQQLREKLREekTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEF 603
Cdd:TIGR02168 253 EELEELTAELQELEekLEELRLEVSELEEEIEELQKELYA--LANEISRLEQQKQILRERLANLERQLEELEAQLEELES 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 604 KREvQLQAIVKKAQEEEAKVNEIafintLEAQNKRHDVL-SKLKEYEQRLNELqeerqrrqeekqaRDEAVQERKRALEA 682
Cdd:TIGR02168 331 KLD-ELAEELAELEEKLEELKEE-----LESLEAELEELeAELEELESRLEEL-------------EEQLETLRSKVAQL 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 683 ERQarvEELLMKR-KEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIqlKHDESIRRHMEQI 761
Cdd:TIGR02168 392 ELQ---IASLNNEiERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQ--EELERLEEALEEL 466
|
....*....
gi 225579092 762 EQRKEKAAE 770
Cdd:TIGR02168 467 REELEEAEQ 475
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
537-709 |
1.75e-06 |
|
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: 52.26 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 537 KRTIAESKKKHEEKQMKAQQlrEKLREEKtlKLQKLLEREKdvRKWKEELLDQRRRMMEEKLLHAEFKREVQLQaivKKA 616
Cdd:pfam15709 346 RRLEVERKRREQEEQRRLQQ--EQLERAE--KMREELELEQ--QRRFEEIRLRKQRLEEERQRQEEEERKQRLQ---LQA 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 617 QEEEAKVNEIAFINTLE--AQNKRHDVLSKLKEYEQRLNELQEERQRRQEE--KQARDEAVQERKRALEAERQARVEELL 692
Cdd:pfam15709 417 AQERARQQQEEFRRKLQelQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRlmEMAEEERLEYQRQKQEAEEKARLEAEE 496
|
170 180
....*....|....*....|...
gi 225579092 693 MKRKEQEA------RIEQQRQEK 709
Cdd:pfam15709 497 RRQKEEEAarlaleEAMKQAQEQ 519
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
395-710 |
1.97e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.84 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 395 EEKFPAEKARIENEmdpsdisNSMAEVLAKKEEL--ADRLEKANEEAIASAIAEEEQLTReieAEENNDINIETDNDSDF 472
Cdd:PTZ00121 1507 EAKKKADEAKKAEE-------AKKADEAKKAEEAkkADEAKKAEEKKKADELKKAEELKK---AEEKKKAEEAKKAEEDK 1576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 473 SASMGSGSVSFCGMSMDWNDVLADYEARESWRQNtswgDIVEEEPARPPGHGIHMHEKLsspsrKRTIAESKKKHEEKQM 552
Cdd:PTZ00121 1577 NMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE----EAKKAEEAKIKAEELKKAEEE-----KKKVEQLKKKEAEEKK 1647
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 553 KAQQLReKLREEKTLKLQKLLEREKDVRKWKEELL---DQRRRMMEEKLLHAEFKREVQlQAIVKKAQE----EEAKVNE 625
Cdd:PTZ00121 1648 KAEELK-KAEEENKIKAAEEAKKAEEDKKKAEEAKkaeEDEKKAAEALKKEAEEAKKAE-ELKKKEAEEkkkaEELKKAE 1725
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 626 iafintlEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQARVEELLmKRKEQEARIEQQ 705
Cdd:PTZ00121 1726 -------EENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEEL-DEEDEKRRMEVD 1797
|
....*
gi 225579092 706 RQEKE 710
Cdd:PTZ00121 1798 KKIKD 1802
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
535-771 |
2.58e-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: 2.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 535 SRKRTIAESKKKHEEKQMKAQQLREKLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQ-LQAIV 613
Cdd:TIGR02168 295 NEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEeLESRL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 614 KKAQEE-EAKVNEIAfintlEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQARVEELL 692
Cdd:TIGR02168 375 EELEEQlETLRSKVA-----QLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEEL 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 225579092 693 MKRKEQEARIEQQRQEKEKaredaarerardreeRLAALTAAQQEAMEELQKKIQLKHdeSIRRHMEQIEQRKEKAAEL 771
Cdd:TIGR02168 450 EELQEELERLEEALEELRE---------------ELEEAEQALDAAERELAQLQARLD--SLERLQENLEGFSEGVKAL 511
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
573-785 |
2.99e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 2.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 573 LErEKDVRKWKEELLDQRRRM--MEEKLLHAEFKREvQLQAIVKKAQEEEAKVNEIAFINTL-------EAQNKRHDVLS 643
Cdd:COG4913 218 LE-EPDTFEAADALVEHFDDLerAHEALEDAREQIE-LLEPIRELAERYAAARERLAELEYLraalrlwFAQRRLELLEA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 644 KLKEYEQRLNELqeerQRRQEEKQARDEAVQERKRALEAERQA----RVEEL--LMKRKEQE-ARIEQQRQEKEKAREDA 716
Cdd:COG4913 296 ELEELRAELARL----EAELERLEARLDALREELDELEAQIRGnggdRLEQLerEIERLERElEERERRRARLEALLAAL 371
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 225579092 717 ARERARDREERLAALTAAQQ--EAMEELQKKIQLKHDESIRRHMEQIEQRKEKAAELSSGRHANTDYAPKL 785
Cdd:COG4913 372 GLPLPASAEEFAALRAEAAAllEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARL 442
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
535-745 |
3.27e-06 |
|
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: 51.49 E-value: 3.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 535 SRKRTIAEskkKHEEKQMKAQQLREKLREEKTLKlQKLLEREKdvrKWKEEL-LDQRRRMMEEKLlhaefkREVQLQAIV 613
Cdd:pfam15709 334 SRDRLRAE---RAEMRRLEVERKRREQEEQRRLQ-QEQLERAE---KMREELeLEQQRRFEEIRL------RKQRLEEER 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 614 KKAQEEEAKvneiafiNTLEAQNKRHDVLSKLKEYEQRLNELQEerqRRQEEKQARDEAVQERKRALEaERQARVEELLM 693
Cdd:pfam15709 401 QRQEEEERK-------QRLQLQAAQERARQQQEEFRRKLQELQR---KKQQEEAERAEAEKQRQKELE-MQLAEEQKRLM 469
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 225579092 694 KRKEQEaRIEQQRQEKEKAREDAARERARDREERLAAlTAAQQEAMEELQKK 745
Cdd:pfam15709 470 EMAEEE-RLEYQRQKQEAEEKARLEAEERRQKEEEAA-RLALEEAMKQAQEQ 519
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
537-774 |
3.56e-06 |
|
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: 50.92 E-value: 3.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 537 KRTIAESKKKHEEKQMKAQQLREKLREEKtlklQKLLEREKDVRKWKEELLDQRRRM----MEEKLLHAEFKREVQLQAI 612
Cdd:COG4942 33 QQEIAELEKELAALKKEEKALLKQLAALE----RRIAALARRIRALEQELAALEAELaeleKEIAELRAELEAQKEELAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 613 VKKAQEEEAKVNEIAFINTLEAQNKRHDVLSKLKEYEQRLNELQEERqrrqeekQARDEAVQERKRALEAERQaRVEELL 692
Cdd:COG4942 109 LLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEEL-------RADLAELAALRAELEAERA-ELEALL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 693 MKRKEQEARIEQQRQEKEKaredaarerardREERLAALTAAQQEAMEELQKKIQlkhdeSIRRHMEQIEQRKEKAAELS 772
Cdd:COG4942 181 AELEEERAALEALKAERQK------------LLARLEKELAELAAELAELQQEAE-----ELEALIARLEAEAAAAAERT 243
|
..
gi 225579092 773 SG 774
Cdd:COG4942 244 PA 245
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
402-771 |
3.57e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.69 E-value: 3.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 402 KARIENEMDPSDIS--NSMAEVLAKKEELADRLEKAnEEAIASAIAEEEQLTREIEAEENNDINIETDN---DSDFSASM 476
Cdd:COG4717 176 QEELEELLEQLSLAteEELQDLAEELEELQQRLAEL-EEELEEAQEELEELEEELEQLENELEAAALEErlkEARLLLLI 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 477 GSGSVSFCGMSMDWNDVLAdyeareswrqnTSWGDIVEEEPARPPGHGIHMHEKLSSPSRKRTIAESKKKHEEKQMKAQQ 556
Cdd:COG4717 255 AAALLALLGLGGSLLSLIL-----------TIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEE 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 557 LREKLREEKTLKLQKLLEREKDVRKWKEeLLDQRRRMMEEKLLHAEFKREVQLQAIVKKAQEEEakvneiaFINTLEAQN 636
Cdd:COG4717 324 LLAALGLPPDLSPEELLELLDRIEELQE-LLREAEELEEELQLEELEQEIAALLAEAGVEDEEE-------LRAALEQAE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 637 KRHDVLSKLKEYEQRLNELqeerqrrqeekqaRDEAVQERKRALEAERQARVEELLMKRKEQEARIEQQRQEKEKAREDA 716
Cdd:COG4717 396 EYQELKEELEELEEQLEEL-------------LGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAEL 462
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 225579092 717 ARERARDREERLAALTAAQQEAMEELQKKIQLKH--DESIRRHMEQIEQRK-----EKAAEL 771
Cdd:COG4717 463 EQLEEDGELAELLQELEELKAELRELAEEWAALKlaLELLEEAREEYREERlppvlERASEY 524
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
537-765 |
3.95e-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: 3.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 537 KRTIAESKKKHEEKQMKAQQLREKLREEKTLK-----LQKLLEREKDVR-----KWKEELldQRRRMMEEKLLHAEFKRE 606
Cdd:pfam13868 108 ERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQaewkeLEKEEEREEDERileylKEKAER--EEEREAEREEIEEEKERE 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 607 VQ-LQAIVKKAQEEEAKVNEIAFINTLEAQNKRHdvlsKLKEYEQRLNELQEERQRrqeeKQARDEAVQERKRALEAERQ 685
Cdd:pfam13868 186 IArLRAQQEKAQDEKAERDELRAKLYQEEQERKE----RQKEREEAEKKARQRQEL----QQAREEQIELKERRLAEEAE 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 686 -ARVEELLMKRKEQEA-RIEQQRQEKEKAREDAARERARDREERLAAL-TAAQQEAMEELQKKIQLkhDESIRRHMEQIE 762
Cdd:pfam13868 258 rEEEEFERMLRKQAEDeEIEQEEAEKRRMKRLEHRRELEKQIEEREEQrAAEREEELEEGERLREE--EAERRERIEEER 335
|
...
gi 225579092 763 QRK 765
Cdd:pfam13868 336 QKK 338
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
437-952 |
4.17e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.68 E-value: 4.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 437 EEAIASAIAEEEQLTREIeaeenNDINIETDNDSDFSASMGSGSVSFCGMSMDWNDVLADYEARESWRQNTSWGdivEEE 516
Cdd:PTZ00121 1030 EELTEYGNNDDVLKEKDI-----IDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFG---KAE 1101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 517 PARPPGHGIHMHEKLSSPSRKRtiAESKKKHEEKQmKAQQLR--EKLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMM 594
Cdd:PTZ00121 1102 EAKKTETGKAEEARKAEEAKKK--AEDARKAEEAR-KAEDARkaEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKA 1178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 595 EEKLLHAEFKR--EVQLQAIVKKAQ-----EEEAKVNEI-AFINTLEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEK 666
Cdd:PTZ00121 1179 EAARKAEEVRKaeELRKAEDARKAEaarkaEEERKAEEArKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFE 1258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 667 QARDEAVQERKRALEAERQARVEELLMKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKI 746
Cdd:PTZ00121 1259 EARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKA 1338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 747 Q--LKHDESIRRHMEQIEQRKEKAAELSSGRHANTDYAPKLTPYERKKqcslcnvliSSEVYLFSHVKgRKHQQAVRENT 824
Cdd:PTZ00121 1339 EeaKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKK---------AEEKKKADEAK-KKAEEDKKKAD 1408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 825 SIQGRELSDEEVEHLSLKkyiidiVVESTAPAEALKDGEERQknkkkakkikarmnfRAKEYESLMETKNSGSDSPYKAK 904
Cdd:PTZ00121 1409 ELKKAAAAKKKADEAKKK------AEEKKKADEAKKKAEEAK---------------KADEAKKKAEEAKKAEEAKKKAE 1467
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 225579092 905 LQRLAKDLLKQVQVQDSGSWANNKVSALDRTLGEITRILEKENVADQI 952
Cdd:PTZ00121 1468 EAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEA 1515
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
537-711 |
8.21e-06 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 50.60 E-value: 8.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 537 KRTIAESKKKHEEKQMKAQQLREKLrEEKTLKLQKLLereKDVRKWKEELLDQRRRM--MEEKLLHaefKREVQLQAIVK 614
Cdd:PRK00409 508 KKLIGEDKEKLNELIASLEELEREL-EQKAEEAEALL---KEAEKLKEELEEKKEKLqeEEDKLLE---EAEKEAQQAIK 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 615 KAQEEEAKVneIAFINTLEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKR-------------ALE 681
Cdd:PRK00409 581 EAKKEADEI--IKELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELKVGDEvkylslgqkgevlSIP 658
|
170 180 190
....*....|....*....|....*....|
gi 225579092 682 AERQARVEELLMKRKEQEARIEQQRQEKEK 711
Cdd:PRK00409 659 DDKEAIVQAGIMKMKVPLSDLEKIQKPKKK 688
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
544-747 |
1.54e-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: 48.76 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 544 KKKHEEKQMKAQQLREKLREEKTLKLQKLLEREKDVRKWKEELLDqrRRMMEEkllHAEFKREVQLQAIVKKAQEEEakv 623
Cdd:pfam13868 164 KAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRA--KLYQEE---QERKERQKEREEAEKKARQRQ--- 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 624 nEIAFINTLEAQNKRHdVLSKLKEYEQRLNElqeerqrrqeeKQARDEAVQERKRALEAERQArveellMKRKEQEARIE 703
Cdd:pfam13868 236 -ELQQAREEQIELKER-RLAEEAEREEEEFE-----------RMLRKQAEDEEIEQEEAEKRR------MKRLEHRRELE 296
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 225579092 704 QQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQ 747
Cdd:pfam13868 297 KQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKKLK 340
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
535-711 |
1.75e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.29 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 535 SRKRTIAESKKKHEEKQMKAQQLREKLR------EEKTLKLQKLLEREKDV-------------RKWKEELLDQRRRMme 595
Cdd:PRK03918 235 ELKEEIEELEKELESLEGSKRKLEEKIReleeriEELKKEIEELEEKVKELkelkekaeeyiklSEFYEEYLDELREI-- 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 596 EKLLHaefKREVQLQAIVKKAQEEEAKVNEIAFINTLEAQNKRHdvLSKLKEYEQRLNELQEERQRRQEEKQAR-DEAVQ 674
Cdd:PRK03918 313 EKRLS---RLEEEINGIEERIKELEEKEERLEELKKKLKELEKR--LEELEERHELYEEAKAKKEELERLKKRLtGLTPE 387
|
170 180 190
....*....|....*....|....*....|....*....
gi 225579092 675 ERKRALEAERQAR--VEELLMKRKEQEARIEQQRQEKEK 711
Cdd:PRK03918 388 KLEKELEELEKAKeeIEEEISKITARIGELKKEIKELKK 426
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
560-949 |
2.92e-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: 48.81 E-value: 2.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 560 KLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKllhAEFKREVQLQAIVKKAQEEEAKVNEIAF--------INT 631
Cdd:pfam02463 169 RKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQA---KKALEYYQLKEKLELEEEYLLYLDYLKLneeridllQEL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 632 LEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAE-----RQARVEELLMKRKEQEARIEQQR 706
Cdd:pfam02463 246 LRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEElkselLKLERRKVDDEEKLKESEKEKKK 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 707 QEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLkhdESIRRHMEQIEQRKEKAAELSSGRhantDYAPKLT 786
Cdd:pfam02463 326 AEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEK---LEQLEEELLAKKKLESERLSSAAK----LKEEELE 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 787 PYERKKQCSLCNVLISSEvyLFSHVKGRKHQQAV------RENTSIQGRELSDEEVEHLSLKKYIIDIVVESTAPAEALK 860
Cdd:pfam02463 399 LKSEEEKEAQLLLELARQ--LEDLLKEEKKEELEileeeeESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKE 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 861 D---GEERQKNKKKAKKIKARMNFRAKEYESLMETKNSGSDSPYKAKLQRLAKDLLKQVQVQDSGSWANNKVSALDRTLG 937
Cdd:pfam02463 477 TqlvKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSAT 556
|
410
....*....|..
gi 225579092 938 EITRILEKENVA 949
Cdd:pfam02463 557 ADEVEERQKLVR 568
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
494-785 |
4.26e-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: 47.34 E-value: 4.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 494 LADYEARESWRQNTSWGDIVEEEPARPpghgihmHEKLSspsRKRTIAESKKKHEEKQMKAQQ-LREKLREEKTLKLQKL 572
Cdd:pfam15558 81 RADRREKQVIEKESRWREQAEDQENQR-------QEKLE---RARQEAEQRKQCQEQRLKEKEeELQALREQNSLQLQER 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 573 LEREKDVRKWKEELLDQRRRM--MEEKLLHAEFKREVQLQAivkKAQEEEAKvneiafiNTLE-----AQNKRHDVLskl 645
Cdd:pfam15558 151 LEEACHKRQLKEREEQKKVQEnnLSELLNHQARKVLVDCQA---KAEELLRR-------LSLEqslqrSQENYEQLV--- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 646 keyEQRLNELQEerqrrqeekQARDEAVQERK---RALEAERQaRVEELLMKRKEQEARIEQQRQEKEKAREdaarerar 722
Cdd:pfam15558 218 ---EERHRELRE---------KAQKEEEQFQRakwRAEEKEEE-RQEHKEALAELADRKIQQARQVAHKTVQ-------- 276
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 225579092 723 DREERLAALTAAQQEAMEELQKKIQLKHDESIRRHMEQIEQRKEKAAELSSGRHANTDYAPKL 785
Cdd:pfam15558 277 DKAQRARELNLEREKNHHILKLKVEKEEKCHREGIKEAIKKKEQRSEQISREKEATLEEARKT 339
|
|
| Stathmin |
pfam00836 |
Stathmin family; The Stathmin family of proteins play an important role in the regulation of ... |
520-626 |
4.70e-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: 44.65 E-value: 4.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 520 PPGHGIHMHEKLSSPSRKRTIAESKkkheEKQMKAQQLREKLREEKTLK-LQKLLEREKDVRKWKEELLDQRRRMMEEKL 598
Cdd:pfam00836 23 PPSVNAAPPKLSLSPKKKDSSLEEI----QKKLEAAEERRKSLEAQKLKqLAEKREKEEEALQKADEENNNFSKMAEEKL 98
|
90 100 110
....*....|....*....|....*....|..
gi 225579092 599 LHA----EFKREVQLQAIVKKAQEEEAKVNEI 626
Cdd:pfam00836 99 KQKmeayKENREAQIAALKEKLKEKEKHVEEV 130
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
534-770 |
4.94e-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: 47.34 E-value: 4.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 534 PSRKRTIAE---SKKKHEEKQMKAQQLREKLREEKTLKLQKLLEREKDVRKWkeeLLDQRRRMMEEKLlhAEFKREVQlq 610
Cdd:pfam15558 3 PERDRKIAAlmlARHKEEQRMRELQQQAALAWEELRRRDQKRQETLERERRL---LLQQSQEQWQAEK--EQRKARLG-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 611 aivkkaQEEEAKVnEIAFINTLEAQNKRHDVLSKlKEyEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQArvEE 690
Cdd:pfam15558 76 ------REERRRA-DRREKQVIEKESRWREQAED-QE-NQRQEKLERARQEAEQRKQCQEQRLKEKEEELQALREQ--NS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 691 LLMKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQL--KHDESIRRHMEQIEQR---- 764
Cdd:pfam15558 145 LQLQERLEEACHKRQLKEREEQKKVQENNLSELLNHQARKVLVDCQAKAEELLRRLSLeqSLQRSQENYEQLVEERhrel 224
|
....*.
gi 225579092 765 KEKAAE 770
Cdd:pfam15558 225 REKAQK 230
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
529-770 |
5.10e-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: 48.04 E-value: 5.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 529 EKLSSPSRKRTIAESKKKHEEKQMKAQQlREKLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQ 608
Cdd:pfam02463 301 ELLKLERRKVDDEEKLKESEKEKKKAEK-ELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKK 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 609 LQAIVKKAQEEEAKVNEIAFINTLEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQARV 688
Cdd:pfam02463 380 KLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELK 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 689 EELLMKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIrrhmeQIEQRKEKA 768
Cdd:pfam02463 460 LLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRII-----SAHGRLGDL 534
|
..
gi 225579092 769 AE 770
Cdd:pfam02463 535 GV 536
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
529-711 |
5.74e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 5.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 529 EKLSSPS-RKRTIAESKKKHEEKQMKAQQLREKLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMmeekllhaefKREV 607
Cdd:COG4717 56 DELFKPQgRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL----------EKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 608 QLQAIVKKAQEEEAKVNEIAfintleaqnkrhDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQAR 687
Cdd:COG4717 126 QLLPLYQELEALEAELAELP------------ERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEE 193
|
170 180
....*....|....*....|....
gi 225579092 688 VEELLMKRKEQEARIEQQRQEKEK 711
Cdd:COG4717 194 LQDLAEELEELQQRLAELEEELEE 217
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
592-770 |
6.16e-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: 46.84 E-value: 6.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 592 RMMEEKLLHAEFKREVQLQAIVKKAQEEEAKvneiafintleAQNKRHDVLSKlkeyEQRLNELQEERQRRQEEKQARDE 671
Cdd:pfam13868 9 RELNSKLLAAKCNKERDAQIAEKKRIKAEEK-----------EEERRLDEMME----EERERALEEEEEKEEERKEERKR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 672 AVQERKRALEAERQARVEELLMKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTA-AQQEAMEELQKKIQLKH 750
Cdd:pfam13868 74 YRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFnEEQAEWKELEKEEEREE 153
|
170 180
....*....|....*....|
gi 225579092 751 DESIRRHMEQIEQRKEKAAE 770
Cdd:pfam13868 154 DERILEYLKEKAEREEEREA 173
|
|
| ZnF_U1 |
smart00451 |
U1-like zinc finger; Family of C2H2-type zinc fingers, present in matrin, U1 small nuclear ... |
790-822 |
6.47e-05 |
|
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: 41.47 E-value: 6.47e-05
10 20 30
....*....|....*....|....*....|...
gi 225579092 790 RKKQCSLCNVLISSEVYLFSHVKGRKHQQAVRE 822
Cdd:smart00451 2 GGFYCKLCNVTFTDEISVEAHLKGKKHKKNVKK 34
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
401-713 |
1.04e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 46.40 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 401 EKARIENEMDPSDISNSMAEVLAKKEELADRLEKANEeaiaSAIAEEEQ--LTREIEAEENNDINIETDNDsdfsasmgs 478
Cdd:pfam02029 18 ERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSG----QGGLDEEEafLDRTAKREERRQKRLQEALE--------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 479 GSVSFCGMSMDWNDVLADYEARESWRQNTSW--GDIVEEEPARPPGHGIHMHEKLSSPSRKRTIAESKKKHEEKQMKAQQ 556
Cdd:pfam02029 85 RQKEFDPTIADEKESVAERKENNEEEENSSWekEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEEEGEEEEDKSE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 557 LREKLREEKTLKLQKLLEREKDVRKWKEE---LLDQRRRMMEEKLLHAEF---------KREVQLQAIVKKAQEEEAKVN 624
Cdd:pfam02029 165 EAEEVPTENFAKEEVKDEKIKKEKKVKYEskvFLDQKRGHPEVKSQNGEEevtklkvttKRRQGGLSQSQEREEEAEVFL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 625 EIAfiNTLEAQNKRHDVLSKlKEYEQRLNELQEERQRRQEEKQARdeavQERKRALEAERQARVEEllmkRKEQEARIEQ 704
Cdd:pfam02029 245 EAE--QKLEELRRRRQEKES-EEFEKLRQKQQEAELELEELKKKR----EERRKLLEEEEQRRKQE----EAERKLREEE 313
|
....*....
gi 225579092 705 qrqEKEKAR 713
Cdd:pfam02029 314 ---EKRRMK 319
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
544-772 |
1.42e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 46.50 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 544 KKKHEEKQMKAQQLREKLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQLQAIVKKAQEEEAKV 623
Cdd:TIGR00618 657 QERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAA 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 624 NEIAFINTL-EAQNKRHDVLSKLKEYEQRLNElqeerqrRQEEKQARDEAVQERKRALEAERQARvEELLMKRKEQEARI 702
Cdd:TIGR00618 737 REDALNQSLkELMHQARTVLKARTEAHFNNNE-------EVTAALQTGAELSHLAAEIQFFNRLR-EEDTHLLKTLEAEI 808
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 225579092 703 EQQRQEKEKAREDAARERARDRE---ERLAALTAAQQEAmeelqkKIQLKHDESIRRHMEQIEQRKEKAAELS 772
Cdd:TIGR00618 809 GQEIPSDEDILNLQCETLVQEEEqflSRLEEKSATLGEI------THQLLKYEECSKQLAQLTQEQAKIIQLS 875
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
536-792 |
2.86e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 536 RKRTIAESKKKHEEKQMKAQQLRE---------KLREEKTLKLQKLLEREKDVRKWKEELLDQRRRM-----MEEKL--- 598
Cdd:PRK03918 264 LEERIEELKKEIEELEEKVKELKElkekaeeyiKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIkeleeKEERLeel 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 599 --LHAEFKREV-QLQAIVKKAQEEEAKVNEIAFINTLEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQE 675
Cdd:PRK03918 344 kkKLKELEKRLeELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKE 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 676 RKRALEAERQAR-------------------------VEELLMKRKEQEARIEQQRQEKEKAREDAARERARDREERLAa 730
Cdd:PRK03918 424 LKKAIEELKKAKgkcpvcgrelteehrkelleeytaeLKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELA- 502
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 225579092 731 ltaaqqEAMEELQKKIQLKHDESIRRHMEQIEQRKEKAAELSSGRHANTDYAPKLTPYERKK 792
Cdd:PRK03918 503 ------EQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKL 558
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
553-773 |
2.96e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 553 KAQQLREKLREEKtlklQKLLEREKDVRKWKEELLDQRRRmmEEKLLHA----EFKREVQLQAIVKKAQEEEAKVNEI-A 627
Cdd:PRK02224 409 NAEDFLEELREER----DELREREAELEATLRTARERVEE--AEALLEAgkcpECGQPVEGSPHVETIEEDRERVEELeA 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 628 FINTLEAQ----NKRHDVLSKLKEYEQR----------LNELQEERQRRQEEKQARDEAVQERKRALEAERQARVEELLM 693
Cdd:PRK02224 483 ELEDLEEEveevEERLERAEDLVEAEDRierleerredLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAE 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 694 KRKE-QEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIRRhmEQIEQRKEKAAELS 772
Cdd:PRK02224 563 AEEEaEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERR--ERLAEKRERKRELE 640
|
.
gi 225579092 773 S 773
Cdd:PRK02224 641 A 641
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
531-764 |
3.20e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 3.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 531 LSSPSRKRTIAESK---KKHEEKQMKAQQLREKLREEKTlKLQKLLEREKDVRKWKEeLLDQRRRMmEEKLlhaefkREV 607
Cdd:PRK03918 445 LTEEHRKELLEEYTaelKRIEKELKEIEEKERKLRKELR-ELEKVLKKESELIKLKE-LAEQLKEL-EEKL------KKY 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 608 QLQAIVKKAQEEEaKVNEIAfiNTLEAQnkrhdvLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQAR 687
Cdd:PRK03918 516 NLEELEKKAEEYE-KLKEKL--IKLKGE------IKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFES 586
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 688 VEELLMKRKE---------------QEARIEQQRQEKEKAREDAARERARDREERLAALTaaqqEAMEELQKKIQLKHDE 752
Cdd:PRK03918 587 VEELEERLKElepfyneylelkdaeKELEREEKELKKLEEELDKAFEELAETEKRLEELR----KELEELEKKYSEEEYE 662
|
250
....*....|..
gi 225579092 753 SIRRHMEQIEQR 764
Cdd:PRK03918 663 ELREEYLELSRE 674
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
554-780 |
3.29e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 45.03 E-value: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 554 AQQLREKLREEKTLKlQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQLQAIVKKAQEEEAKVNeiafintLE 633
Cdd:COG3064 1 AQEALEEKAAEAAAQ-ERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAE-------LA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 634 AQNKRhdvlsKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQARVEELLmKRKEQEARIEQQRQEKEKAR 713
Cdd:COG3064 73 AEAAK-----KLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAK-RKAEEEAKRKAEEERKAAEA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 225579092 714 EDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIRRHMEQIEQRKEKAAELSSGRHANTD 780
Cdd:COG3064 147 EAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAAD 213
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
498-771 |
3.36e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 44.86 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 498 EARESWRQntswgdivEEEPARPPGHGIHMHEKLSSPSRKRTIAESKKKHEEKQMKAQQLReKLREEKTLKLQKLLEREK 577
Cdd:pfam02029 17 EERRRQKE--------EEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTA-KREERRQKRLQEALERQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 578 D----VRKWKEELLDQRRRMMEEKLLHAEFKREVQlqaivkkAQEEEAKVNEIAFINTLEAQNKRHDVLSKLKEYEQRLN 653
Cdd:pfam02029 88 EfdptIADEKESVAERKENNEEEENSSWEKEEKRD-------SRLGRYKEEETEIREKEYQENKWSTEVRQAEEEGEEEE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 654 ELQEERQRRQEEKQARDEAVQERKRALEAERQARVEELLMKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTA 733
Cdd:pfam02029 161 DKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEA 240
|
250 260 270
....*....|....*....|....*....|....*....
gi 225579092 734 AQQEAMEELQKKIQLKHDESIRRHMEQIEQRK-EKAAEL 771
Cdd:pfam02029 241 EVFLEAEQKLEELRRRRQEKESEEFEKLRQKQqEAELEL 279
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
540-768 |
4.13e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.01 E-value: 4.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 540 IAESKKKHEEKQMKAQQLREK-----LREEKTLKLQKLLErekdvrkwkeelLDQRRRMMEEKLLHAEFKREvQLQAIVK 614
Cdd:COG3206 184 LPELRKELEEAEAALEEFRQKnglvdLSEEAKLLLQQLSE------------LESQLAEARAELAEAEARLA-ALRAQLG 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 615 KAQEEEAKVNEIAFINTLEAQnkRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQARVEELLMK 694
Cdd:COG3206 251 SGPDALPELLQSPVIQQLRAQ--LAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAR 328
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 225579092 695 RKEQEARIEQQRQEkekaredaarerardreerLAALTAAQQEaMEELQKKIQLKhdesiRRHMEQIEQRKEKA 768
Cdd:COG3206 329 EASLQAQLAQLEAR-------------------LAELPELEAE-LRRLEREVEVA-----RELYESLLQRLEEA 377
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
666-793 |
5.00e-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: 44.56 E-value: 5.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 666 KQARDEAVQERKRALEAE-RQARVEEllmKRKEQEariEQQRQEKEKAREDAARErardreerlAALTAAQQEAMEELQK 744
Cdd:pfam15709 327 KREQEKASRDRLRAERAEmRRLEVER---KRREQE---EQRRLQQEQLERAEKMR---------EELELEQQRRFEEIRL 391
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 225579092 745 KIQLKHDESIRRHMEQIEQRKEKAAELSSGRHANTDYAPKLTPYERKKQ 793
Cdd:pfam15709 392 RKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQ 440
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
540-738 |
5.03e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 5.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 540 IAESKKKHEEKQMKAQQLREKLR------EEKTLKLQKLLEREKDVRKWKEELldqrrrmmEEKLLHAEfKREVQLQAIV 613
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDalqaelEELNEEYNELQAELEALQAEIDKL--------QAEIAEAE-AEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 614 KK----AQEEEAKVNEIAFIntLEAQN-----KRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAER 684
Cdd:COG3883 89 GEraraLYRSGGSVSYLDVL--LGSESfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAEL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 225579092 685 QARVEELLMKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEA 738
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220
|
|
| zf-met |
pfam12874 |
Zinc-finger of C2H2 type; This is a zinc-finger domain with the CxxCx(12)Hx(6)H motif, found ... |
794-816 |
5.08e-04 |
|
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: 38.63 E-value: 5.08e-04
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
556-771 |
5.11e-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: 44.14 E-value: 5.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 556 QLREKLREEKTLKLQKLLEREKDVRKwKEELLDQRR--RMMEEKLLHAEFKREvqlqaivkkaQEEEAKVNE-IAFINTL 632
Cdd:pfam13868 10 ELNSKLLAAKCNKERDAQIAEKKRIK-AEEKEEERRldEMMEEERERALEEEE----------EKEEERKEErKRYRQEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 633 EAQNKRHDVLsKLKEYEQRLNElqeerqrrqeeKQARDEAVQERKRALEAERQARVEELLMKRKEQEARIEQQRQEKEKa 712
Cdd:pfam13868 79 EEQIEEREQK-RQEEYEEKLQE-----------REQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKEL- 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 225579092 713 redaarerardreerlaaltaaQQEAMEELQKKIQ----LKHDESIRRHMEQIEQRKEKAAEL 771
Cdd:pfam13868 146 ----------------------EKEEEREEDERILeylkEKAEREEEREAEREEIEEEKEREI 186
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
532-771 |
5.35e-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: 5.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 532 SSPSRKRTIAESKKKHEEKQmkaqqlreklREEKTLKLQKLLEREKDVR-KWKEELLDQRRRMMEEKLLHAEFKREVQlq 610
Cdd:pfam15709 297 SSPTQTFVVTGNMESEEERS----------EEDPSKALLEKREQEKASRdRLRAERAEMRRLEVERKRREQEEQRRLQ-- 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 611 aivKKAQEEEAKVNEiafinTLEAQNKRHDVLSKLKEyeQRLNElqeerqrrQEEKQARDEAVQERKRALEAERqARVEE 690
Cdd:pfam15709 365 ---QEQLERAEKMRE-----ELELEQQRRFEEIRLRK--QRLEE--------ERQRQEEEERKQRLQLQAAQER-ARQQQ 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 691 LLMKRKEQEarIEQQRQEKEKAREDAARERARDREERLAA-----LTAAQQEAMEELQKKiqLKHDESIRRHMEQIEQRK 765
Cdd:pfam15709 426 EEFRRKLQE--LQRKKQQEEAERAEAEKQRQKELEMQLAEeqkrlMEMAEEERLEYQRQK--QEAEEKARLEAEERRQKE 501
|
....*.
gi 225579092 766 EKAAEL 771
Cdd:pfam15709 502 EEAARL 507
|
|
| CCDC47 |
pfam07946 |
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ... |
666-749 |
5.39e-04 |
|
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: 43.71 E-value: 5.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 666 KQARDEAVQERKRALEAERQarvEELLMKRKEQEarieqqRQEKEKaredaarerardreeRLAALTAAQQEAMEELQKK 745
Cdd:pfam07946 263 KKTREEEIEKIKKAAEEERA---EEAQEKKEEAK------KKEREE---------------KLAKLSPEEQRKYEEKERK 318
|
....
gi 225579092 746 IQLK 749
Cdd:pfam07946 319 KEQR 322
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
529-986 |
5.60e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 44.26 E-value: 5.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 529 EKLSSPSRKRTIAESKKKHEEKQMKAQQLREK----LREEKTLKLQKLLEREKDVRKWKEElLDQRRRMMEEKLLHAEFK 604
Cdd:COG3064 3 EALEEKAAEAAAQERLEQAEAEKRAAAEAEQKakeeAEEERLAELEAKRQAEEEAREAKAE-AEQRAAELAAEAAKKLAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 605 REVQLQAIVKKAQEEEAKVNEiafintlEAQnkrhdvlsklkeyEQRLNELQEERQRRQEEKQARDEAVQERKRALEAER 684
Cdd:COG3064 82 AEKAAAEAEKKAAAEKAKAAK-------EAE-------------AAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEER 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 685 QARVEELLMKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIRRHMEQIEQR 764
Cdd:COG3064 142 KAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAV 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 765 KEKAAELSSGRHANTDYAPKLTPYERKKQcslcnvliSSEVYLFSHVKGRKHQQAVRENTSIQGRELSDEEVEHLSLKKY 844
Cdd:COG3064 222 AARAAAASREAALAAVEATEEAALGGAEE--------AADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAA 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 845 IIDIVVESTAPAEALKDGEERQKNKKKAKKIKARMNFRAKE--YESLMETKNSGSDSPYKAKLQRLAKDLLKQVQVQDSG 922
Cdd:COG3064 294 GLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGAasLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAG 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 225579092 923 SWANNKVSALDRTLGEITRILEKENVADQIAFQAAGGLTALEHILQAVVPATNVNTVLRIPPKS 986
Cdd:COG3064 374 ALLLGKLADVEEAAGAGILAAAGGGGLLGLRLDLGAALLEAASAVELRVLLALAGAAGAVVALL 437
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
535-709 |
6.41e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 6.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 535 SRKRTIAESKKKHEEKQMKAQQLREKLREEKTlKLQKLLEREKDVRKWKEELLDQRRRMME------EKLLHAEFKRE-- 606
Cdd:PRK03918 228 KEVKELEELKEEIEELEKELESLEGSKRKLEE-KIRELEERIEELKKEIEELEEKVKELKElkekaeEYIKLSEFYEEyl 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 607 VQLQAIVKKAQEEEAKVNEI-AFINTLEAQNKRHDVLSK-LKEYEQRLNELQEERQRRQEEKQARDEAVQERKR--ALEA 682
Cdd:PRK03918 307 DELREIEKRLSRLEEEINGIeERIKELEEKEERLEELKKkLKELEKRLEELEERHELYEEAKAKKEELERLKKRltGLTP 386
|
170 180
....*....|....*....|....*...
gi 225579092 683 ERQARVEELLMKRKEQ-EARIEQQRQEK 709
Cdd:PRK03918 387 EKLEKELEELEKAKEEiEEEISKITARI 414
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
536-655 |
8.35e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.16 E-value: 8.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 536 RKRTIAESKKKHEEKQMKAQQLREKLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREV-QLQAIVK 614
Cdd:COG1196 659 GGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLeAEREELL 738
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 225579092 615 KAQEEEAKVNEIAFINTLEAQNKRHDVLSKLKEYEQRLNEL 655
Cdd:COG1196 739 EELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
538-945 |
8.58e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.80 E-value: 8.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 538 RTIAESKKKHEEKQMKAQQLREKLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQLQAIVKKAQ 617
Cdd:TIGR00618 462 QESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLE 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 618 EEEAKVNEI-------AFINTLEAQNKRHDvLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQARVEE 690
Cdd:TIGR00618 542 TSEEDVYHQltserkqRASLKEQMQEIQQS-FSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRK 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 691 LLMKRKEQEARIE----QQRQEKEkaredaarerardreerlaaLTAAQQEAMEELQKKIQLKHDESIRRHMEQIEQRKE 766
Cdd:TIGR00618 621 LQPEQDLQDVRLHlqqcSQELALK--------------------LTALHALQLTLTQERVREHALSIRVLPKELLASRQL 680
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 767 KAAELSSGRHANTDYAPKLTPYERKKQCSLCNVLISS----EVYLFSHVKGRK-HQQAVRENTSIQG-RELSDEEVEHLS 840
Cdd:TIGR00618 681 ALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDrefnEIENASSSLGSDlAAREDALNQSLKElMHQARTVLKART 760
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 841 LkkyiIDIVVESTAPAEALKDGEERQKNKKKAkkikarmNFRAKEYESLMETKNSGSDSPYKAKLQRLAKDLLKQVQVQD 920
Cdd:TIGR00618 761 E----AHFNNNEEVTAALQTGAELSHLAAEIQ-------FFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQE 829
|
410 420
....*....|....*....|....*
gi 225579092 921 SGSwANNKVSALDRTLGEITRILEK 945
Cdd:TIGR00618 830 EEQ-FLSRLEEKSATLGEITHQLLK 853
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
548-711 |
8.73e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 43.26 E-value: 8.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 548 EEKQMKAQQLREKLREEKTLKLQKLLEREKDVRKWK-EELLDQRRRMMEEKLLHAEFKREVQLQAivKKAQEEEAKVNEI 626
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERlKQLEKERLAAQEQKKQAEEAAKQAALKQ--KQAEEAAAKAAAA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 627 AFINTlEAQNKRHDVLSKLKEYEQRLNElqeerqrrqeEKQARDEAVQERKRALEAERQARVEELLMKRKEQEARIEQQR 706
Cdd:PRK09510 145 AKAKA-EAEAKRAAAAAKKAAAEAKKKA----------EAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAA 213
|
....*
gi 225579092 707 QEKEK 711
Cdd:PRK09510 214 EAKKK 218
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
547-711 |
9.26e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 9.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 547 HEEKQMKAQQLREKLREEKTlKLQKLLEREKDVRKwKEELLDQRRRMMEEKLLHAEFKREVQLQAivkkaqeeeakvnEI 626
Cdd:COG4913 283 LWFAQRRLELLEAELEELRA-ELARLEAELERLEA-RLDALREELDELEAQIRGNGGDRLEQLER-------------EI 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 627 AfintlEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERqARVEELLMKRKEQEARIEQQR 706
Cdd:COG4913 348 E-----RLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEEL-EALEEALAEAEAALRDLRREL 421
|
....*
gi 225579092 707 QEKEK 711
Cdd:COG4913 422 RELEA 426
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
549-777 |
1.12e-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: 42.98 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 549 EKQMKAQQLREKLREEKTLKLQKLLEREkDVRKWKEELLDQRRRMMEEKLLHAEFKREVQLQAIvKKAQEEEAKVNEIAF 628
Cdd:pfam13868 25 DAQIAEKKRIKAEEKEEERRLDEMMEEE-RERALEEEEEKEEERKEERKRYRQELEEQIEEREQ-KRQEEYEEKLQEREQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 629 INTLEAQNKRHDvlskLKEYEQRLNElqeerqrrQEE-KQARDEAVQERKRALEAERQA------RVEELLMKRKEQEAR 701
Cdd:pfam13868 103 MDEIVERIQEED----QAEAEEKLEK--------QRQlREEIDEFNEEQAEWKELEKEEereedeRILEYLKEKAEREEE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 225579092 702 IEQQRQEKEKaredaARERARDREERLAALTAAQQEAMEEL-QKKIQLKHDESIR-RHMEQIEQRKEKAAELSSGRHA 777
Cdd:pfam13868 171 REAEREEIEE-----EKEREIARLRAQQEKAQDEKAERDELrAKLYQEEQERKERqKEREEAEKKARQRQELQQAREE 243
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
568-773 |
1.44e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 568 KLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQLQAIVKKAQEEEAKVNEIafINTLE-----AQNKRHDVL 642
Cdd:PRK02224 163 KLEEYRERASDARLGVERVLSDQRGSLDQLKAQIEEKEEKDLHERLNGLESELAELDEE--IERYEeqreqARETRDEAD 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 643 SKLKEYEQRLNE----------LQEERQRRQEEKQARDEAVQERKRA---LEAERQARVEELLMKRKEQEArIEQQRQEK 709
Cdd:PRK02224 241 EVLEEHEERREEletleaeiedLRETIAETEREREELAEEVRDLRERleeLEEERDDLLAEAGLDDADAEA-VEARREEL 319
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 225579092 710 EKAREDAARErardreerLAALTAAQQEAMEELQKkiqlkHDESIRRHMEQIEQRKEKAAELSS 773
Cdd:PRK02224 320 EDRDEELRDR--------LEECRVAAQAHNEEAES-----LREDADDLEERAEELREEAAELES 370
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
529-927 |
2.32e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 42.76 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 529 EKLSSPSRKRTIAESKKKHEEKQMKAQQLREKLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFK--RE 606
Cdd:COG5022 820 IKLQKTIKREKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSISslKL 899
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 607 VQLQ------AIVKKAQEEEAKVNEI--AFINTLEAQNKRHDV-LSKLKEYEQ--RLNELqeerqrrQEEKQARDEAVQE 675
Cdd:COG5022 900 VNLEleseiiELKKSLSSDLIENLEFktELIARLKKLLNNIDLeEGPSIEYVKlpELNKL-------HEVESKLKETSEE 972
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 676 RKRAL----EAERQARVEELLMKRKEQEArieqQRQEKEKAREDAARERARDREERLAALTAAQQEAMEE-LQKKIQLKH 750
Cdd:COG5022 973 YEDLLkkstILVREGNKANSELKNFKKEL----AELSKQYGALQESTKQLKELPVEVAELQSASKIISSEsTELSILKPL 1048
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 751 DESIRRHMEQIEQRKEKAAELSSGRhANTDYAPKLTpYERKKQCSLCNVLISSEVYLFS--HVKGRKHQQAVRENTSIQG 828
Cdd:COG5022 1049 QKLKGLLLLENNQLQARYKALKLRR-ENSLLDDKQL-YQLESTENLLKTINVKDLEVTNrnLVKPANVLQFIVAQMIKLN 1126
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 829 reLSDEEVEHLSLKKYIIDIVVESTAPAEALKDGEERQKNKKKAKKIKARMNFRAKE--YESLMETKNSGSDS------- 899
Cdd:COG5022 1127 --LLQEISKFLSQLVNTLEPVFQKLSVLQLELDGLFWEANLEALPSPPPFAALSEKRlyQSALYDEKSKLSSSevndlkn 1204
|
410 420
....*....|....*....|....*...
gi 225579092 900 PYKAKLQRLAKDLLKQVQVQDSGSWANN 927
Cdd:COG5022 1205 ELIALFSKIFSGWPRGDKLKKLISEGWV 1232
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
556-704 |
2.33e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.19 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 556 QLREKLREEKTL-----KLQKLLEREKDVRKWKEELLDQRRRMMEEKLlhAEFKREvqLQAIVKKAQEEEAKVNEIAFIN 630
Cdd:pfam07888 35 RLEECLQERAELlqaqeAANRQREKEKERYKRDREQWERQRRELESRV--AELKEE--LRQSREKHEELEEKYKELSASS 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 225579092 631 TLEAQNKrhDVLSKLK-EYEQRLNELQEERqrrqeekQARDEAVQERKRALEAERQaRVEELLMKRKEQEARIEQ 704
Cdd:pfam07888 111 EELSEEK--DALLAQRaAHEARIRELEEDI-------KTLTQRVLERETELERMKE-RAKKAGAQRKEEEAERKQ 175
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
537-655 |
2.75e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 537 KRTIAESKKKHEEKQMKAQQLREKLREEKTLKLQKLLEREkdvrkwkEELLDQRRRMMEEKLLHAEFKREvQLQAIVKKA 616
Cdd:COG1579 58 EKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEALQKE-------IESLKRRISDLEDEILELMERIE-ELEEELAEL 129
|
90 100 110
....*....|....*....|....*....|....*....
gi 225579092 617 QEEEAKVNEiafinTLEAQNKRHDvlSKLKEYEQRLNEL 655
Cdd:COG1579 130 EAELAELEA-----ELEEKKAELD--EELAELEAELEEL 161
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
536-626 |
3.80e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 41.12 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 536 RKRTIAESKKKHEEKQMKAQQLREKLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQLQAIVKK 615
Cdd:pfam02841 202 KEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERSYQEHVKQLIEKMEAEREQLLAEQERMLEHKLQEQEELLKEG 281
|
90
....*....|..
gi 225579092 616 AQEE-EAKVNEI 626
Cdd:pfam02841 282 FKTEaESLQKEI 293
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
645-771 |
4.06e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 4.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 645 LKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEaERQARVEELLMKRKEQEARIEQQRQEKEKAREDAARERARDR 724
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAE-EKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 225579092 725 EERLAALTAAQQEAMEELQKKIQ--LKHDESIRRHMEQIEQRKEKAAEL 771
Cdd:COG4717 127 LLPLYQELEALEAELAELPERLEelEERLEELRELEEELEELEAELAEL 175
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
539-711 |
4.63e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 4.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 539 TIAESKKKHEEKQMKAQQLREKLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMME-EKLLHAEFKREVQLQAIVKKAQ 617
Cdd:COG4372 28 ALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEElNEQLQAAQAELAQAQEELESLQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 618 EEEAKVNEIafINTLEAQNKrhdvlsKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAE-RQARVEELLMKRK 696
Cdd:COG4372 108 EEAEELQEE--LEELQKERQ------DLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEElAALEQELQALSEA 179
|
170
....*....|....*
gi 225579092 697 EQEARIEQQRQEKEK 711
Cdd:COG4372 180 EAEQALDELLKEANR 194
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
670-774 |
5.17e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 40.64 E-value: 5.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 670 DEAVQERKRALEAER-QARVEELLMKR-KEQEARIEQQRQEKEKAredaarerardreerlaaltaaQQEAMEELQKKIQ 747
Cdd:cd16269 190 DQALTEKEKEIEAERaKAEAAEQERKLlEEQQRELEQKLEDQERS----------------------YEEHLRQLKEKME 247
|
90 100
....*....|....*....|....*...
gi 225579092 748 LKHDESIRRHMEQIEQR-KEKAAELSSG 774
Cdd:cd16269 248 EERENLLKEQERALESKlKEQEALLEEG 275
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
400-747 |
6.53e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.08 E-value: 6.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 400 AEKARIENEMDPSDISNSMAEVLAKKEELADRLEKANEEAIASAIAEEEQLTREIEAEENNDINIETDNDSDFSASMGSg 479
Cdd:COG1196 419 LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL- 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 480 svsfcgmSMDWNDVLADYEARESWRQNTSWG----------DIVEEEPARPPGHGIHMHEKLSSPSR--KRTIAESKKKH 547
Cdd:COG1196 498 -------EAEADYEGFLEGVKAALLLAGLRGlagavavligVEAAYEAALEAALAAALQNIVVEDDEvaAAAIEYLKAAK 570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 548 EEKQMKAQQLREKLREEKTLKLQKLL----------EREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQLQAIVKKAQ 617
Cdd:COG1196 571 AGRATFLPLDKIRARAALAAALARGAigaavdlvasDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVT 650
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 618 EEEAKVNEIAFIntLEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQARVEELLMKRKE 697
Cdd:COG1196 651 LEGEGGSAGGSL--TGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEE 728
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 225579092 698 QEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEaMEELQKKIQ 747
Cdd:COG1196 729 QLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERE-LERLEREIE 777
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
559-771 |
6.57e-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: 41.21 E-value: 6.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 559 EKLREEktlkLQKLLEREKDVRKWKEELLDQRRRMMEEKLlHAEfkrevQLQAIVKKAQEEEAKVnEIAFINTLEAQNKR 638
Cdd:TIGR02169 173 EKALEE----LEEVEENIERLDLIIDEKRQQLERLRRERE-KAE-----RYQALLKEKREYEGYE-LLKEKEALERQKEA 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 639 HDV-LSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQARVEELLMKRKEQEARIEQQRQEKEKAREDAA 717
Cdd:TIGR02169 242 IERqLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAE 321
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 225579092 718 RErardrEERLAALTAAQQEAMEELQKKIQlkhDESIRRH--MEQIEQRKEKAAEL 771
Cdd:TIGR02169 322 ER-----LAKLEAEIDKLLAEIEELEREIE---EERKRRDklTEEYAELKEELEDL 369
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
540-752 |
8.19e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.89 E-value: 8.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 540 IAESKKKHEEKQMKAQQLREKLREEKTlKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAE----FKREVQLQAIVKK 615
Cdd:COG1340 73 VKELKEERDELNEKLNELREELDELRK-ELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEekelVEKIKELEKELEK 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 616 AQEEEAKVNEIAFINT--LEAQNKRHDVLSKLKEYEQRLNELQEERQRRqeeKQARDEAVQERKRALEA--ERQARVEEL 691
Cdd:COG1340 152 AKKALEKNEKLKELRAelKELRKEAEEIHKKIKELAEEAQELHEEMIEL---YKEADELRKEADELHKEivEAQEKADEL 228
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 225579092 692 lmkRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDE 752
Cdd:COG1340 229 ---HEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAEEIFEKLKKGEKLTTEE 286
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
532-769 |
8.21e-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: 40.72 E-value: 8.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 532 SSPSRKRTIAESKKKHEEKQMKAQQLREKLREEKTLKLQKLlerekdvrKWKEELLDQRRRMME---EKLLHAEFKREVQ 608
Cdd:TIGR00618 216 TYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQL--------KKQQLLKQLRARIEElraQEAVLEETQERIN 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 609 LQAIVKKAQEEEAKVNEIAF----INTL--EAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQ----ARDEAVQERKR 678
Cdd:TIGR00618 288 RARKAAPLAAHIKAVTQIEQqaqrIHTElqSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSqeihIRDAHEVATSI 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 679 ALEAERQARVEELLMKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIRRHM 758
Cdd:TIGR00618 368 REISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAI 447
|
250
....*....|....
gi 225579092 759 E---QIEQRKEKAA 769
Cdd:TIGR00618 448 TctaQCEKLEKIHL 461
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
575-770 |
8.85e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 8.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 575 REKDVRKWKeelldQRRRMM----EEKLlhAEFKREV-QLQAIVKKAQEEEAKVNEIafintLEAQNKRHDVLSKLKEY- 648
Cdd:COG4913 590 HEKDDRRRI-----RSRYVLgfdnRAKL--AALEAELaELEEELAEAEERLEALEAE-----LDALQERREALQRLAEYs 657
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 649 --EQRLNELQEERQRRQEEKQARD------EAVQERKRALEAERQA---RVEELLMKRKEQEARIEQQRQEKEKAREDAA 717
Cdd:COG4913 658 wdEIDVASAEREIAELEAELERLDassddlAALEEQLEELEAELEEleeELDELKGEIGRLEKELEQAEEELDELQDRLE 737
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 225579092 718 RERARDREERLAALTAA-QQEAMEELQKKIQlkhdESIRRHMEQIEQRKEKAAE 770
Cdd:COG4913 738 AAEDLARLELRALLEERfAAALGDAVERELR----ENLEERIDALRARLNRAEE 787
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
667-770 |
8.93e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 40.17 E-value: 8.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 667 QARDEAVQERKRALEAERQARVEEllMKRKEQEARI--EQQRQEKEKAREDAARERARDREERLAALTAAQQeAMEELQK 744
Cdd:PRK09510 93 QQKQAAEQERLKQLEKERLAAQEQ--KKQAEEAAKQaaLKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKK-AAAEAKK 169
|
90 100
....*....|....*....|....*.
gi 225579092 745 KiqlkhdesirrhmEQIEQRKEKAAE 770
Cdd:PRK09510 170 K-------------AEAEAAKKAAAE 182
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
535-711 |
9.07e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 9.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 535 SRKRTIAESKKKHEEKQMKAQQLREKLREEKTL--KLQKLLEREKDVRKWKEEL--LDQRRRMMEE---KLLHAEfKREV 607
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERREAlqRLAEYSWDEIDVASAEREIaeLEAELERLDAssdDLAALE-EQLE 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 608 QLQAIVKKAQEEEAKVNEIAFintlEAQNKRHDVLSKLKEYEQRLNElqeerqrrqeekqARDEAVQERKRALEAERQAR 687
Cdd:COG4913 696 ELEAELEELEEELDELKGEIG----RLEKELEQAEEELDELQDRLEA-------------AEDLARLELRALLEERFAAA 758
|
170 180
....*....|....*....|....
gi 225579092 688 VEELLMKRKEQEARIEQQRQEKEK 711
Cdd:COG4913 759 LGDAVERELRENLEERIDALRARL 782
|
|
| ARGLU |
pfam15346 |
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ... |
541-625 |
9.56e-03 |
|
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is required for the oestrogen-dependent expression of ESR1 target genes. It functions in cooperation with MED1. The family of proteins is found in eukaryotes.
Pssm-ID: 405931 [Multi-domain] Cd Length: 151 Bit Score: 38.11 E-value: 9.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 541 AESKKKHEEKQMKAQQLRE--------KLREEKTLKLQKLLEREKDVRKWKEEllDQRRRMMEEKLLHAEFKREVQLQAI 612
Cdd:pfam15346 43 VEEARKIMEKQVLEELEREreaeleeeRRKEEEERKKREELERILEENNRKIE--EAQRKEAEERLAMLEEQRRMKEERQ 120
|
90
....*....|...
gi 225579092 613 VKKAQEEEAKVNE 625
Cdd:pfam15346 121 RREKEEEEREKRE 133
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
535-711 |
9.62e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.52 E-value: 9.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 535 SRKRTIAESKKKHEEKQMKAQQLREKLREEKTLKLQKLLEREKDVRKwKEELLDQRRRMMEekllhaefKREVQLQAiVK 614
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKR-LELEIEEVEARIK--------KYEEQLGN-VR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225579092 615 KAQEEEAKVNEIafintlEAQNKRHDVLSK-LKEYEQRLNELqeerqrrqeekqardEAVQERKRALEAERQARVEELLM 693
Cdd:COG1579 87 NNKEYEALQKEI------ESLKRRISDLEDeILELMERIEEL---------------EEELAELEAELAELEAELEEKKA 145
|
170
....*....|....*...
gi 225579092 694 KRKEQEARIEQQRQEKEK 711
Cdd:COG1579 146 ELDEELAELEAELEELEA 163
|
|
| |
