|
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 ... |
1-52 |
3.52e-23 |
|
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: 95.17 E-value: 3.52e-23
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1211848747 1 MMLDNYVRDFKALIDWIQLQEKLEKTDAQSRPTSLAWEVKKMSPGRHVIPSP 52
Cdd:pfam16501 47 MVLDNYTRDFKALIEWFRLKWDYENTPPPQRPTSLAWEVRKSSPGKSVNKSP 98
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
403-637 |
3.80e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.12 E-value: 3.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 403 KRTIAESKKKHEEKQMKAQQLREKLREEkTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQLQAIVKKA 482
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEEL-ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 483 QEEEAKVNEIAFINTL-EAQNKRHDVLSKLKEYEQRLNELqeerqrRQEEKQARDEAVQERKRALEAERQARVEELLMKR 561
Cdd:COG1196 331 ELEELEEELEELEEELeEAEEELEEAEAELAEAEEALLEA------EAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1211848747 562 KEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQkKIQLKHDESIRRHMEQIEQRKEKAAEL 637
Cdd:COG1196 405 LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA-ELEEEEEALLELLAELLEEAALLEAAL 479
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
258-636 |
5.06e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 70.94 E-value: 5.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 258 QVNEEKFPAEKARIENEMDPSDISNSMAEVLAKKEELADRLEKANEEAIASAIAEEEQLTREiEAEENNDinietdndsd 337
Cdd:PTZ00121 1432 KADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAE-EAKKKAD---------- 1500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 338 fsasmgsgsvsfcgmsmdwndvladyEARESWRQNTSWGDIVEEEPARPPGHGIHMHEKLSSPSRKRtiAESKKKHEEKQ 417
Cdd:PTZ00121 1501 --------------------------EAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKK--AEEKKKADELK 1552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 418 mKAQQLReKLREEKTLKLQKLLEREKDVRKWKEELLDQ--RRRMMEEKLLHAEFKREVQLQAivKKAQEEEAKVNEIafi 495
Cdd:PTZ00121 1553 -KAEELK-KAEEKKKAEEAKKAEEDKNMALRKAEEAKKaeEARIEEVMKLYEEEKKMKAEEA--KKAEEAKIKAEEL--- 1625
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 496 NTLEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARD--EAVQERKRALE---AERQARVEELLMKRKEQEARIEQ 570
Cdd:PTZ00121 1626 KKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEakKAEEDKKKAEEakkAEEDEKKAAEALKKEAEEAKKAE 1705
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1211848747 571 QRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIRRHMEQIEQRKEKAAE 636
Cdd:PTZ00121 1706 ELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAE 1771
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
415-636 |
3.79e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.65 E-value: 3.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 415 EKQMKAQQLREKLRE-EKTLKLQKLLEREKDVRKWKEELLDQRRRmmEEKLLHAEFKREVQLQAIVKKAQEEEAKVNEia 493
Cdd:COG1196 210 EKAERYRELKEELKElEAELLLLKLRELEAELEELEAELEELEAE--LEELEAELAELEAELEELRLELEELELELEE-- 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 494 fintleAQNKRHDVLSKLKEYEQRLNELQeerQRRQEEKQARDEAVQERKRALE--AERQARVEELLMKRKEQEARIEQQ 571
Cdd:COG1196 286 ------AQAEEYELLAELARLEQDIARLE---ERRRELEERLEELEEELAELEEelEELEEELEELEEELEEAEEELEEA 356
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1211848747 572 RQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIRRHMEQIEQRKEKAAE 636
Cdd:COG1196 357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
211-577 |
1.16e-10 |
|
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: 66.24 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 211 QFTVSTLDD--VKNSGSIRDNYVRTSEISAVHIDTECVSVMLQAGTPPLQVNEEKFPAEKARIENEMDP-----SDISNS 283
Cdd:TIGR02169 638 KYRMVTLEGelFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDElsqelSDASRK 717
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 284 MAEVLAKKEELADRLEKANEEaiasaIAEEEQLTREIEAEENNDINIETDNDSDFSAsmgsgsvsfcgMSMDWNDV---L 360
Cdd:TIGR02169 718 IGEIEKEIEQLEQEEEKLKER-----LEELEEDLSSLEQEIENVKSELKELEARIEE-----------LEEDLHKLeeaL 781
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 361 ADYEARES---WRQNTSWGDIVEEEPARPPGHGIHMHEKLSSPSRKRTIAESKKKHEEKQMKAQQLREKLREEK----TL 433
Cdd:TIGR02169 782 NDLEARLShsrIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEienlNG 861
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 434 KLQKLLEREKDVRKWKEELLDQRRRMMEEKLlhaefKREVQLQAIVKKAQEEEAKVnEIAFINTLEAQNKRHDVLSKLKE 513
Cdd:TIGR02169 862 KKEELEEELEELEAALRDLESRLGDLKKERD-----ELEAQLRELERKIEELEAQI-EKKRKRLSELKAKLEALEEELSE 935
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 514 YEQRLNELQEERQRRQEEK--QARDEAVQERKRALE----------AERQARVEELLMK-------RKEQEARIEQQRQE 574
Cdd:TIGR02169 936 IEDPKGEDEEIPEEELSLEdvQAELQRVEEEIRALEpvnmlaiqeyEEVLKRLDELKEKrakleeeRKAILERIEEYEKK 1015
|
...
gi 1211848747 575 KEK 577
Cdd:TIGR02169 1016 KRE 1018
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
403-795 |
1.68e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.93 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 403 KRTIAESKKKHEEKQmKAQQLREKLREEKtlKLQKLLEREKDVRKWKEEL---------LDQRRRMMEEKLLHAEFKREV 473
Cdd:PTZ00121 1456 AKKAEEAKKKAEEAK-KADEAKKKAEEAK--KADEAKKKAEEAKKKADEAkkaaeakkkADEAKKAEEAKKADEAKKAEE 1532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 474 QLQAIVKKAQEEEAKVNEIAFINTLEAQNKRHDVLSKLKEYEQRLNELqeerQRRQEEKQARDEAVQERKRALEAERQAR 553
Cdd:PTZ00121 1533 AKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMAL----RKAEEAKKAEEARIEEVMKLYEEEKKMK 1608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 554 VEELlmkRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDEsirrhmeqiEQRKEK 633
Cdd:PTZ00121 1609 AEEA---KKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKA---------EEDKKK 1676
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 634 AAELSSGRHANTDYAPKLTPYERKKQcslcnvlISSEVYLFSHVKGRKHQQAVR--ENTSIQGRELSDEEVEhlslkkyi 711
Cdd:PTZ00121 1677 AEEAKKAEEDEKKAAEALKKEAEEAK-------KAEELKKKEAEEKKKAEELKKaeEENKIKAEEAKKEAEE-------- 1741
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 712 idivvESTAPAEALKDGEERQKNKKKAKKIKARMNFRAKEYESLMETKNSGSDSPYKAKLQRLAKDLLKQVQVQDSGSWA 791
Cdd:PTZ00121 1742 -----DKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKE 1816
|
....
gi 1211848747 792 NNKV 795
Cdd:PTZ00121 1817 GNLV 1820
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
289-633 |
2.47e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 65.06 E-value: 2.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 289 AKKEELADRLEK---ANEEAIASAIAEEEQLTREIEA--EENNDINIETDNDSDFSASMGSgsvsfcgmsmDWNDVLADY 363
Cdd:PRK02224 359 EELREEAAELESeleEAREAVEDRREEIEELEEEIEElrERFGDAPVDLGNAEDFLEELRE----------ERDELRERE 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 364 EARESWRQNTSwGDIVEEEPARPPGHGIHMHEKLSSPSRKRTIAESKKKHEEKQMKAQQLREKL--------REEKTLKL 435
Cdd:PRK02224 429 AELEATLRTAR-ERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVeeveerleRAEDLVEA 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 436 QKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKR----------EVQLQAIVKKAQEEEAKVNEIAFIN--------T 497
Cdd:PRK02224 508 EDRIERLEERREDLEELIAERRETIEEKRERAEELReraaeleaeaEEKREAAAEAEEEAEEAREEVAELNsklaelkeR 587
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 498 LEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQ---ERKRALEAERQ-ARVEELLMKRKEQEARIEQQRQ 573
Cdd:PRK02224 588 IESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAekrERKRELEAEFDeARIEEAREDKERAEEYLEQVEE 667
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1211848747 574 EkekaredaarerardreerLAALTaaqqEAMEELQKKI-----QLKHDESIRRHMEQIEQRKEK 633
Cdd:PRK02224 668 K-------------------LDELR----EERDDLQAEIgavenELEELEELRERREALENRVEA 709
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
396-576 |
1.05e-09 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 62.83 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 396 KLSSPSRKRTIAESKKKHEEKQMKAQQLRE----KLREEKTLKLQKL----LEREKDVRKWKEELLDQRRRMMEeklLHA 467
Cdd:pfam17380 405 KILEEERQRKIQQQKVEMEQIRAEQEEARQrevrRLEEERAREMERVrleeQERQQQVERLRQQEEERKRKKLE---LEK 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 468 EFKREVQLQAIVKKAQEEEAKVNEIAFIntlEAQNKRHDVLsklKEYEQRLNELQEerqrrqeeKQARDEAVQERKRALE 547
Cdd:pfam17380 482 EKRDRKRAEEQRRKILEKELEERKQAMI---EEERKRKLLE---KEMEERQKAIYE--------EERRREAEEERRKQQE 547
|
170 180
....*....|....*....|....*....
gi 1211848747 548 AERQARVEELLMKRKEQEARIEQQRQEKE 576
Cdd:pfam17380 548 MEERRRIQEQMRKATEERSRLEAMERERE 576
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
402-636 |
1.10e-09 |
|
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: 61.47 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 402 RKRTIAESKKKHEEKQMKAQQLREKLREEKtLKLQKLLEREKDvrkwkEELLDQRRRMMEEKLLHAEFKREVQLQAIVKK 481
Cdd:pfam13868 71 RKRYRQELEEQIEEREQKRQEEYEEKLQER-EQMDEIVERIQE-----EDQAEAEEKLEKQRQLREEIDEFNEEQAEWKE 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 482 AQEEEAKVNE---IAFINTLEAQNKRHDVLSKLKEY--EQRLNELQEERQRRQEEKQARDEAVQER-KRALEAERQARVE 555
Cdd:pfam13868 145 LEKEEEREEDeriLEYLKEKAEREEEREAEREEIEEekEREIARLRAQQEKAQDEKAERDELRAKLyQEEQERKERQKER 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 556 ELLMKRKEQEARI----EQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKK--IQLKHDESIRRHMEQIEQ 629
Cdd:pfam13868 225 EEAEKKARQRQELqqarEEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRrmKRLEHRRELEKQIEEREE 304
|
....*..
gi 1211848747 630 RKEKAAE 636
Cdd:pfam13868 305 QRAAERE 311
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
401-730 |
1.28e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.24 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 401 SRKRTIAESKKKHEEKQmKAQQLREKLREEKtlKLQKLLEREKDVRKWKEELldqrRRMMEEKLLHAEFKR---EVQLQA 477
Cdd:PTZ00121 1362 AEEKAEAAEKKKEEAKK-KADAAKKKAEEKK--KADEAKKKAEEDKKKADEL----KKAAAAKKKADEAKKkaeEKKKAD 1434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 478 IVKKAQEEEAKVNEIafiNTLEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQArvEEl 557
Cdd:PTZ00121 1435 EAKKKAEEAKKADEA---KKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAA--EA- 1508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 558 lmKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIRRHMEQIEQRKEKAAEL 637
Cdd:PTZ00121 1509 --KKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEA 1586
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 638 SSGRHANTDYAPKLTPYERKKQCSlcnvlissevylfshvKGRKHQQAVRENTSIQGRELSDEEVEHLSLKKyiidivVE 717
Cdd:PTZ00121 1587 KKAEEARIEEVMKLYEEEKKMKAE----------------EAKKAEEAKIKAEELKKAEEEKKKVEQLKKKE------AE 1644
|
330
....*....|...
gi 1211848747 718 STAPAEALKDGEE 730
Cdd:PTZ00121 1645 EKKKAEELKKAEE 1657
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
401-630 |
2.84e-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: 2.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 401 SRKRTIAESKKKHEEKQMKAQQLREKLREEKTLKLQKLLEREKDVRKWKEEL--LDQRRRMMEEKLLHAEFKREVQLQAI 478
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELeeAEEELEEAEAELAEAEEALLEAEAEL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 479 VKKAQEEEAKVNEIAfiNTLEAQNKRHDVLSKLKEYEQRLNELqeeRQRRQEEKQARDEAVQERKRALEAERQARVEELL 558
Cdd:COG1196 375 AEAEEELEELAEELL--EALRAAAELAAQLEELEEAEEALLER---LERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1211848747 559 MKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIRRHMEQIEQR 630
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRG 521
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
406-638 |
3.28e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.49 E-value: 3.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 406 IAESKKKHEEKQMKAQQLREKLRE------EKTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQLQAIV 479
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYEllaelaRLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 480 KKAQEEEAKVNEIAFINTL-EAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQARvEELL 558
Cdd:COG1196 349 AEEELEEAEAELAEAEEALlEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEEL-EELE 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 559 MKRKEQEARIEQQRQEKEKaredaarerARDREERLAALTAAQQEAMEELQKKIQLKHDESIRRHMEQIEQRKEKAAELS 638
Cdd:COG1196 428 EALAELEEEEEEEEEALEE---------AAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
395-637 |
1.87e-08 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 58.34 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 395 EKLSSPSRKRTIAESKKKHEEKQMKAQQLREKLREEKTLKLqkllEREKDVRKWKEELLDQRRRMMEEKLLHAEFKrEVQ 474
Cdd:pfam02029 96 EKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIR----EKEYQENKWSTEVRQAEEEGEEEEDKSEEAE-EVP 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 475 LQAIVKKAQEEEAKVNEIAFINTLEA--QNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERqa 552
Cdd:pfam02029 171 TENFAKEEVKDEKIKKEKKVKYESKVflDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQ-- 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 553 RVEELLMKRKEQEAR-IEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKkiQLKHDESIRRHMEQIEQRK 631
Cdd:pfam02029 249 KLEELRRRRQEKESEeFEKLRQKQQEAELELEELKKKREERRKLLEEEEQRRKQEEAER--KLREEEEKRRMKEEIERRR 326
|
....*.
gi 1211848747 632 EKAAEL 637
Cdd:pfam02029 327 AEAAEK 332
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
403-636 |
2.31e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.54 E-value: 2.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 403 KRTIAESKKKHEEKQMKAQQLREKLRE---EKTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEF-KREVQLQAI 478
Cdd:PRK03918 171 IKEIKRRIERLEKFIKRTENIEELIKEkekELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIeELEKELESL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 479 VKKAQEEEAKVNEI-AFINTLEAQnkrhdvLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQE------RKRALEAERQ 551
Cdd:PRK03918 251 EGSKRKLEEKIRELeERIEELKKE------IEELEEKVKELKELKEKAEEYIKLSEFYEEYLDElreiekRLSRLEEEIN 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 552 ArVEELLMKRKEQEARIEQQRQEKEKAREDAARERARDREERLAaltAAQQEAMEELQKKIQLKHDESIRRHMEQIEQRK 631
Cdd:PRK03918 325 G-IEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEA---KAKKEELERLKKRLTGLTPEKLEKELEELEKAK 400
|
....*
gi 1211848747 632 EKAAE 636
Cdd:PRK03918 401 EEIEE 405
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
408-636 |
5.00e-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: 57.76 E-value: 5.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 408 ESKKKHEEKQM-KAQQLREKLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQ--LQAIVKKAQE 484
Cdd:TIGR02168 199 ERQLKSLERQAeKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEekLEELRLEVSE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 485 EEAKVNEI--------AFINTLEAQ-----NKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERq 551
Cdd:TIGR02168 279 LEEEIEELqkelyalaNEISRLEQQkqilrERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLE- 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 552 ARVEELLMKRKEQEARIEQQRQEKEKaredaarerardreerLAALTAAQQEAMEELQKKIQlkhdeSIRRHMEQIEQRK 631
Cdd:TIGR02168 358 AELEELEAELEELESRLEELEEQLET----------------LRSKVAQLELQIASLNNEIE-----RLEARLERLEDRR 416
|
....*
gi 1211848747 632 EKAAE 636
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 ... |
408-636 |
6.61e-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: 57.29 E-value: 6.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 408 ESKKKHEEKQMKAQQLREKLREEKTLKlqKLLEREKD-----VRKWKEELLDQRRRMMEEKLLHAEFKREVQ-------- 474
Cdd:pfam02463 174 ALKKLIEETENLAELIIDLEELKLQEL--KLKEQAKKaleyyQLKEKLELEEEYLLYLDYLKLNEERIDLLQellrdeqe 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 475 ----LQAIVKKAQEEEAKVNEIAFINT--LEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEA 548
Cdd:pfam02463 252 eiesSKQEIEKEEEKLAQVLKENKEEEkeKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 549 ERQARVEELLMKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQ--EAMEELQKKIQLKH-DESIRRHME 625
Cdd:pfam02463 332 KEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERlsSAAKLKEEELELKSeEEKEAQLLL 411
|
250
....*....|.
gi 1211848747 626 QIEQRKEKAAE 636
Cdd:pfam02463 412 ELARQLEDLLK 422
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
402-636 |
7.34e-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: 56.08 E-value: 7.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 402 RKRTIAESKK----KHEEKQMKAQQLREKLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLL-HAEFKRE-VQL 475
Cdd:pfam13868 24 RDAQIAEKKRikaeEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEeYEEKLQErEQM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 476 QAIVKKAQEEEAKVNEIAFI---NTLEAQNKRHDVLSKLKEYE-QRLNELQEERQRRQEEKQARDEAVQERKRALEAERQ 551
Cdd:pfam13868 104 DEIVERIQEEDQAEAEEKLEkqrQLREEIDEFNEEQAEWKELEkEEEREEDERILEYLKEKAEREEEREAEREEIEEEKE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 552 ARVEELLmkrkEQEARIEQQRQEKEKaredaarerardreeRLAALTAAQQEA------MEELQKKIQLKHD--ESIRRH 623
Cdd:pfam13868 184 REIARLR----AQQEKAQDEKAERDE---------------LRAKLYQEEQERkerqkeREEAEKKARQRQElqQAREEQ 244
|
250
....*....|...
gi 1211848747 624 MEQIEQRKEKAAE 636
Cdd:pfam13868 245 IELKERRLAEEAE 257
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
408-636 |
1.37e-07 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 55.90 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 408 ESKKKHEEKQMKAQQL--REKLREEKTLKlQKLLEREKDVRKWKEELLDQRRRMMEeKLLHAEFKREVQlqaivKKAQEE 485
Cdd:pfam17380 297 EQERLRQEKEEKAREVerRRKLEEAEKAR-QAEMDRQAAIYAEQERMAMERERELE-RIRQEERKRELE-----RIRQEE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 486 EA----KVNEIAFINtLEAQNKRHDVLSKLK-------EYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQ--- 551
Cdd:pfam17380 370 IAmeisRMRELERLQ-MERQQKNERVRQELEaarkvkiLEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERArem 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 552 ARVEELLMKRKEQEARIEQQRQE-------KEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIRRHM 624
Cdd:pfam17380 449 ERVRLEEQERQQQVERLRQQEEErkrkkleLEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKA 528
|
250
....*....|..
gi 1211848747 625 EQIEQRKEKAAE 636
Cdd:pfam17380 529 IYEEERRREAEE 540
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
401-636 |
1.87e-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: 55.83 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 401 SRKRTIAESKKKHEEKQMKAQQLREKLREektlKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQ------ 474
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAE----LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEqleeri 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 475 --LQAIVKKAQEEEAKVNEiafiNTLEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALeAERQA 552
Cdd:TIGR02168 750 aqLSKELTELEAEIEELEE----RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA-ANLRE 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 553 RVEELLMKRKEQEARIEQQRQEKEKaredaarerARDREERLAALTAAQQEAMEELQKKIQLKHDE--SIRRHMEQIEQR 630
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEEQIEE---------LSEDIESLAAEIEELEELIEELESELEALLNEraSLEEALALLRSE 895
|
....*.
gi 1211848747 631 KEKAAE 636
Cdd:TIGR02168 896 LEELSE 901
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
405-783 |
3.65e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.15 E-value: 3.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 405 TIAESKKKHEEKQMKaqqlrEKLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMMEEkllhAEFKREVQLQAIVKKAqe 484
Cdd:PTZ00121 1092 ATEEAFGKAEEAKKT-----ETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEE----ARKAEDAKRVEIARKA-- 1160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 485 EEAKVNEIAfintLEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQARVEELL----MK 560
Cdd:PTZ00121 1161 EDARKAEEA----RKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKkaeeAK 1236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 561 RKEQEA-RIEQQRQEKEKAREDAARERARDREErlAALTAAQQEAMEELQKKIQLKHDESIRRHME--QIEQRKEKAAEL 637
Cdd:PTZ00121 1237 KDAEEAkKAEEERNNEEIRKFEEARMAHFARRQ--AAIKAEEARKADELKKAEEKKKADEAKKAEEkkKADEAKKKAEEA 1314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 638 SSGRHA--NTDYAPKLTPYERKKqcslcnvliSSEVYLFSHVKGRKHQQAVREntsiqgRELSDEEVEHLSLKKYiidiv 715
Cdd:PTZ00121 1315 KKADEAkkKAEEAKKKADAAKKK---------AEEAKKAAEAAKAEAEAAADE------AEAAEEKAEAAEKKKE----- 1374
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1211848747 716 vESTAPAEALKDGEERQKNKKKAKKIKARMNFRAKEYESLMETKNSGSDSPYKAKLQRLAKDLLKQVQ 783
Cdd:PTZ00121 1375 -EAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAE 1441
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
403-646 |
4.14e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 54.69 E-value: 4.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 403 KRTIAESK---KKHEEKQMKAQQLREKLREEKTlKLQKLLEREK-DVRKWKEELLDQRRRMMEekllhaefkrevqlqaI 478
Cdd:TIGR02169 307 ERSIAEKErelEDAEERLAKLEAEIDKLLAEIE-ELEREIEEERkRRDKLTEEYAELKEELED----------------L 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 479 VKKAQEEEAKVNEiafinTLEAQNKRHDVLSKLKEyeqRLNELQEERQRRQEEKQARDEAVQERKRALE------AERQA 552
Cdd:TIGR02169 370 RAELEEVDKEFAE-----TRDELKDYREKLEKLKR---EINELKRELDRLQEELQRLSEELADLNAAIAgieakiNELEE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 553 RVEELLMKRKEQEARIEQQRQEKEKaredaarerardREERLAALTAAQQEAMEELQKKiqlkhdesiRRHMEQIEQRKE 632
Cdd:TIGR02169 442 EKEDKALEIKKQEWKLEQLAADLSK------------YEQELYDLKEEYDRVEKELSKL---------QRELAEAEAQAR 500
|
250
....*....|....
gi 1211848747 633 KAAELSSGRHANTD 646
Cdd:TIGR02169 501 ASEERVRGGRAVEE 514
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
404-636 |
6.58e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 53.63 E-value: 6.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 404 RTIAESKKKHEEKQMKaQQLREKLREEKTLKLQKLLErekdvrkWKEELLDQRRrmmeekllhaEFKREVqlqaivkKAQ 483
Cdd:PRK12704 26 KKIAEAKIKEAEEEAK-RILEEAKKEAEAIKKEALLE-------AKEEIHKLRN----------EFEKEL-------RER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 484 EEEakvneiafintLEAQNKRhdvlskLKEYEQRLNElqeerqrrqeekqaRDEAVQERKRALEAERQ---ARVEELLMK 560
Cdd:PRK12704 81 RNE-----------LQKLEKR------LLQKEENLDR--------------KLELLEKREEELEKKEKeleQKQQELEKK 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1211848747 561 RKEQEARIEQQRQEKEKaredaarerardreerLAALTA--AQQEAMEELQKKIQLKHDESIRRHMEQIEQRKEKAAE 636
Cdd:PRK12704 130 EEELEELIEEQLQELER----------------ISGLTAeeAKEILLEKVEEEARHEAAVLIKEIEEEAKEEADKKAK 191
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
375-630 |
7.58e-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: 52.93 E-value: 7.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 375 WGDIVEEEPARPPGHGIHMHEKLSSPSRKRTIAESKKKHEEKQMKAQQLREK--LREEKTLKLQKLLErEKDVRKWKEEL 452
Cdd:TIGR02794 20 LGSLYHSVKPEPGGGAEIIQAVLVDPGAVAQQANRIQQQKKPAAKKEQERQKklEQQAEEAEKQRAAE-QARQKELEQRA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 453 LDQRRRMMEEKllHAEFKREVQLQAIVKKA-QEEEAKVNEiafintlEAQNKRhdvlsKLKEYEQRLNELQEERQRRQEE 531
Cdd:TIGR02794 99 AAEKAAKQAEQ--AAKQAEEKQKQAEEAKAkQAAEAKAKA-------EAEAER-----KAKEEAAKQAEEEAKAKAAAEA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 532 KQARDEAV----QERKRALEAERQARVEELLMKRKEQEARIEQQRQEK---EKAREDAARERARDREERLAALTAAQQEA 604
Cdd:TIGR02794 165 KKKAEEAKkkaeAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKaeaEAAAAAAAEAERKADEAELGDIFGLASGS 244
|
250 260
....*....|....*....|....*..
gi 1211848747 605 MEELQKKIQLKHDES-IRRHMEQIEQR 630
Cdd:TIGR02794 245 NAEKQGGARGAAAGSeVDKYAAIIQQA 271
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
406-655 |
8.84e-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: 53.59 E-value: 8.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 406 IAESKKKHEEKQMKAQQLR---EKLREEKTLKLqkllEREKDVRKWKEELLDQRRrmmeEKLLHAEFKREVQLQAIVK-- 480
Cdd:pfam17380 353 IRQEERKRELERIRQEEIAmeiSRMRELERLQM----ERQQKNERVRQELEAARK----VKILEEERQRKIQQQKVEMeq 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 481 -KAQEEEAKVNEIafiNTLEAQNKRHDVLSKLKEYE--QRLNELQEERQRRQEEKQARDEavQERKRALEAERQARVEEL 557
Cdd:pfam17380 425 iRAEQEEARQREV---RRLEEERAREMERVRLEEQErqQQVERLRQQEEERKRKKLELEK--EKRDRKRAEEQRRKILEK 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 558 LMKRKEQeARIEQQRQEK--EKAREDAARERARDREERLAALTAAQQEAMEElQKKIQ------------LKHDESIRRH 623
Cdd:pfam17380 500 ELEERKQ-AMIEEERKRKllEKEMEERQKAIYEEERRREAEEERRKQQEMEE-RRRIQeqmrkateersrLEAMEREREM 577
|
250 260 270
....*....|....*....|....*....|....*
gi 1211848747 624 MEQIEQRKEKAAELSSGRHANT---DYAPKLTPYE 655
Cdd:pfam17380 578 MRQIVESEKARAEYEATTPITTikpIYRPRISEYQ 612
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
407-578 |
9.86e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 52.50 E-value: 9.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 407 AESKKKHEEKQMKAQQLREKLREEKTLKLQKLLEREKdvrkwkEELLDQrrrmmEEKLLHAEFKREVQLQAivKKAQEEE 486
Cdd:PRK09510 72 KSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEK------ERLAAQ-----EQKKQAEEAAKQAALKQ--KQAEEAA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 487 AKVNEIAFINTlEAQNKRHDVLSKLKEYEQRLNElqeerqrrqeEKQARDEAVQERKRALEAERQARVEELLMKRKEQEA 566
Cdd:PRK09510 139 AKAAAAAKAKA-EAEAKRAAAAAKKAAAEAKKKA----------EAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEA 207
|
170
....*....|..
gi 1211848747 567 RIEQQRQEKEKA 578
Cdd:PRK09510 208 KKKAAAEAKKKA 219
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
261-576 |
1.76e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.84 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 261 EEKFPAEKARIENEmdpsdisNSMAEVLAKKEEL--ADRLEKANEEAIASAIAEEEQLTReieAEENNDINIETDNDSDF 338
Cdd:PTZ00121 1507 EAKKKADEAKKAEE-------AKKADEAKKAEEAkkADEAKKAEEKKKADELKKAEELKK---AEEKKKAEEAKKAEEDK 1576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 339 SASMGSGSVSFCGMSMDWNDVLADYEARESWRQNtswgDIVEEEPARPPGHGIHMHEKLsspsrKRTIAESKKKHEEKQM 418
Cdd:PTZ00121 1577 NMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE----EAKKAEEAKIKAEELKKAEEE-----KKKVEQLKKKEAEEKK 1647
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 419 KAQQLReKLREEKTLKLQKLLEREKDVRKWKEELL---DQRRRMMEEKLLHAEFKREVQlQAIVKKAQE----EEAKVNE 491
Cdd:PTZ00121 1648 KAEELK-KAEEENKIKAAEEAKKAEEDKKKAEEAKkaeEDEKKAAEALKKEAEEAKKAE-ELKKKEAEEkkkaEELKKAE 1725
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 492 iafintlEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQARVEELLmKRKEQEARIEQQ 571
Cdd:PTZ00121 1726 -------EENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEEL-DEEDEKRRMEVD 1797
|
....*
gi 1211848747 572 RQEKE 576
Cdd:PTZ00121 1798 KKIKD 1802
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
403-575 |
1.93e-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: 51.88 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 403 KRTIAESKKKHEEKQMKAQQlrEKLREEKtlKLQKLLEREKdvRKWKEELLDQRRRMMEEKLLHAEFKREVQLQaivKKA 482
Cdd:pfam15709 346 RRLEVERKRREQEEQRRLQQ--EQLERAE--KMREELELEQ--QRRFEEIRLRKQRLEEERQRQEEEERKQRLQ---LQA 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 483 QEEEAKVNEIAFINTLE--AQNKRHDVLSKLKEYEQRLNELQEERQRRQEE--KQARDEAVQERKRALEAERQARVEELL 558
Cdd:pfam15709 417 AQERARQQQEEFRRKLQelQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRlmEMAEEERLEYQRQKQEAEEKARLEAEE 496
|
170 180
....*....|....*....|...
gi 1211848747 559 MKRKEQEA------RIEQQRQEK 575
Cdd:pfam15709 497 RRQKEEEAarlaleEAMKQAQEQ 519
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
417-643 |
2.10e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.25 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 417 QMKAQQLRE-----------KLREEKTLKlqKL------LEREKDVRkwkEELLDQRRR--------------MMEEKLL 465
Cdd:COG1196 151 EAKPEERRAiieeaagiskyKERKEEAER--KLeateenLERLEDIL---GELERQLEPlerqaekaeryrelKEELKEL 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 466 HAEFK----REVQLQAIVKKAQEEEAKVNEIAFINTLEAQNKRHDVL-SKLKEYEQRLNELqeerqrrqeekQARDEAVQ 540
Cdd:COG1196 226 EAELLllklRELEAELEELEAELEELEAELEELEAELAELEAELEELrLELEELELELEEA-----------QAEEYELL 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 541 ERKRALEAERQaRVEELLMKRKEQEARIEQQRQEKEKAREDAarerardrEERLAALTAAQQEAMEELQKKiQLKHDESI 620
Cdd:COG1196 295 AELARLEQDIA-RLEERRRELEERLEELEEELAELEEELEEL--------EEELEELEEELEEAEEELEEA-EAELAEAE 364
|
250 260
....*....|....*....|...
gi 1211848747 621 RRHMEQIEQRKEKAAELSSGRHA 643
Cdd:COG1196 365 EALLEAEAELAEAEEELEELAEE 387
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
392-636 |
2.49e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.98 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 392 HMHEKLSSPSRKRT--IAESKKKHEEKQMKAQQLREKLREekTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEF 469
Cdd:TIGR02168 253 EELEELTAELQELEekLEELRLEVSELEEEIEELQKELYA--LANEISRLEQQKQILRERLANLERQLEELEAQLEELES 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 470 KREvQLQAIVKKAQEEEAKVNEIafintLEAQNKRHDVL-SKLKEYEQRLNELqeerqrrqeekqarDEAVQERKRALeA 548
Cdd:TIGR02168 331 KLD-ELAEELAELEEKLEELKEE-----LESLEAELEELeAELEELESRLEEL--------------EEQLETLRSKV-A 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 549 ERQARVEELLMKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIqlKHDESIRRHMEQIE 628
Cdd:TIGR02168 390 QLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQ--EELERLEEALEELR 467
|
....*...
gi 1211848747 629 QRKEKAAE 636
Cdd:TIGR02168 468 EELEEAEQ 475
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
439-651 |
3.23e-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: 3.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 439 LErEKDVRKWKEELLDQRRRM--MEEKLLHAEFKREvQLQAIVKKAQEEEAKVNEIAFINTL-------EAQNKRHDVLS 509
Cdd:COG4913 218 LE-EPDTFEAADALVEHFDDLerAHEALEDAREQIE-LLEPIRELAERYAAARERLAELEYLraalrlwFAQRRLELLEA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 510 KLKEYEQRLNELqeerQRRQEEKQARDEAVQERKRALEAERQA----RVEEL--LMKRKEQE-ARIEQQRQEKEKAREDA 582
Cdd:COG4913 296 ELEELRAELARL----EAELERLEARLDALREELDELEAQIRGnggdRLEQLerEIERLERElEERERRRARLEALLAAL 371
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1211848747 583 ARERARDREERLAALTAAQQ--EAMEELQKKIQLKHDESIRRHMEQIEQRKEKAAELSSGRHANTDYAPKL 651
Cdd:COG4913 372 GLPLPASAEEFAALRAEAAAllEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARL 442
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
401-637 |
3.35e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.60 E-value: 3.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 401 SRKRTIAESKKKHEEKQMKAQQLREKLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQ-LQAIV 479
Cdd:TIGR02168 295 NEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEeLESRL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 480 KKAQEE-EAKVNEIAfintlEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQARVEELL 558
Cdd:TIGR02168 375 EELEEQlETLRSKVA-----QLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEEL 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1211848747 559 MKRKEQEARIEQQRQEKEKaredaarerardreeRLAALTAAQQEAMEELQKKIQLKHdeSIRRHMEQIEQRKEKAAEL 637
Cdd:TIGR02168 450 EELQEELERLEEALEELRE---------------ELEEAEQALDAAERELAQLQARLD--SLERLQENLEGFSEGVKAL 511
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
401-611 |
3.73e-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: 51.11 E-value: 3.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 401 SRKRTIAEskkKHEEKQMKAQQLREKLREEKTLKlQKLLEREKdvrKWKEEL-LDQRRRMMEEKLlhaefkREVQLQAIV 479
Cdd:pfam15709 334 SRDRLRAE---RAEMRRLEVERKRREQEEQRRLQ-QEQLERAE---KMREELeLEQQRRFEEIRL------RKQRLEEER 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 480 KKAQEEEAKvneiafiNTLEAQNKRHDVLSKLKEYEQRLNELQEerqRRQEEKQARDEAVQERKRALEaERQARVEELLM 559
Cdd:pfam15709 401 QRQEEEERK-------QRLQLQAAQERARQQQEEFRRKLQELQR---KKQQEEAERAEAEKQRQKELE-MQLAEEQKRLM 469
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1211848747 560 KRKEQEaRIEQQRQEKEKAREDAARERARDREERLAAlTAAQQEAMEELQKK 611
Cdd:pfam15709 470 EMAEEE-RLEYQRQKQEAEEKARLEAEERRQKEEEAA-RLALEEAMKQAQEQ 519
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
303-818 |
3.80e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.68 E-value: 3.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 303 EEAIASAIAEEEQLTREIeaeenNDINIETDNDSDFSASMGSGSVSFCGMSMDWNDVLADYEARESWRQNTSWGdivEEE 382
Cdd:PTZ00121 1030 EELTEYGNNDDVLKEKDI-----IDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFG---KAE 1101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 383 PARPPGHGIHMHEKLSSPSRKRtiAESKKKHEEKQmKAQQLR--EKLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMM 460
Cdd:PTZ00121 1102 EAKKTETGKAEEARKAEEAKKK--AEDARKAEEAR-KAEDARkaEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKA 1178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 461 EEKLLHAEFKR--EVQLQAIVKKAQ-----EEEAKVNEI-AFINTLEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEK 532
Cdd:PTZ00121 1179 EAARKAEEVRKaeELRKAEDARKAEaarkaEEERKAEEArKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFE 1258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 533 QARDEAVQERKRALEAERQARVEELLMKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKI 612
Cdd:PTZ00121 1259 EARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKA 1338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 613 Q--LKHDESIRRHMEQIEQRKEKAAELSSGRHANTDYAPKLTPYERKKqcslcnvliSSEVYLFSHVKgRKHQQAVRENT 690
Cdd:PTZ00121 1339 EeaKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKK---------AEEKKKADEAK-KKAEEDKKKAD 1408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 691 SIQGRELSDEEVEHLSLKkyiidiVVESTAPAEALKDGEERQknkkkakkikarmnfRAKEYESLMETKNSGSDSPYKAK 770
Cdd:PTZ00121 1409 ELKKAAAAKKKADEAKKK------AEEKKKADEAKKKAEEAK---------------KADEAKKKAEEAKKAEEAKKKAE 1467
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1211848747 771 LQRLAKDLLKQVQVQDSGSWANNKVSALDRTLGEITRILEKENVADQI 818
Cdd:PTZ00121 1468 EAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEA 1515
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
403-640 |
4.53e-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: 50.53 E-value: 4.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 403 KRTIAESKKKHEEKQMKAQQLREKLREEKtlklQKLLEREKDVRKWKEELLDQRRRM----MEEKLLHAEFKREVQLQAI 478
Cdd:COG4942 33 QQEIAELEKELAALKKEEKALLKQLAALE----RRIAALARRIRALEQELAALEAELaeleKEIAELRAELEAQKEELAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 479 VKKAQEEEAKVNEIAFINTLEAQNKRHDVLSKLKEYEQRLNELQEERqrrqeekQARDEAVQERKRALEAERQaRVEELL 558
Cdd:COG4942 109 LLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEEL-------RADLAELAALRAELEAERA-ELEALL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 559 MKRKEQEARIEQQRQEKEKaredaarerardREERLAALTAAQQEAMEELQKKIQlkhdeSIRRHMEQIEQRKEKAAELS 638
Cdd:COG4942 181 AELEEERAALEALKAERQK------------LLARLEKELAELAAELAELQQEAE-----ELEALIARLEAEAAAAAERT 243
|
..
gi 1211848747 639 SG 640
Cdd:COG4942 244 PA 245
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
268-631 |
6.83e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 6.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 268 KARIENEMDPSDIS--NSMAEVLAKKEELADRLEKAnEEAIASAIAEEEQLTREIEAEENNDINIETDN---DSDFSASM 342
Cdd:COG4717 176 QEELEELLEQLSLAteEELQDLAEELEELQQRLAEL-EEELEEAQEELEELEEELEQLENELEAAALEErlkEARLLLLI 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 343 GSGSVSFCGMSMDWNDVLAdyeareswrqnTSWGDIVEEEPARPPGHGIHMHEKLSSPSRKRTIAESKKKHEEKQMKAQQ 422
Cdd:COG4717 255 AAALLALLGLGGSLLSLIL-----------TIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEE 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 423 LREKLREEKTLKLQKLLEREKDVRKWKEeLLDQRRRMMEEKLLHAEFKREVQLQAIVKKAQEEEakvneiaFINTLEAQN 502
Cdd:COG4717 324 LLAALGLPPDLSPEELLELLDRIEELQE-LLREAEELEEELQLEELEQEIAALLAEAGVEDEEE-------LRAALEQAE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 503 KRHDVLSKLKEYEQRLNELqeerqrrqeekqaRDEAVQERKRALEAERQARVEELLMKRKEQEARIEQQRQEKEKAREDA 582
Cdd:COG4717 396 EYQELKEELEELEEQLEEL-------------LGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAEL 462
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1211848747 583 ARERARDREERLAALTAAQQEAMEELQKKIQLKH--DESIRRHMEQIEQRK 631
Cdd:COG4717 463 EQLEEDGELAELLQELEELKAELRELAEEWAALKlaLELLEEAREEYREER 513
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
403-631 |
8.93e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 49.53 E-value: 8.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 403 KRTIAESKKKHEEKQMKAQQLREKLREEKTLK-----LQKLLEREKDVR-----KWKEELldQRRRMMEEKLLHAEFKRE 472
Cdd:pfam13868 108 ERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQaewkeLEKEEEREEDERileylKEKAER--EEEREAEREEIEEEKERE 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 473 VQ-LQAIVKKAQEEEAKVNEIAFINTLEAQNKRHdvlsKLKEYEQRLNELQEERQRrqeeKQARDEAVQERKRALEAERQ 551
Cdd:pfam13868 186 IArLRAQQEKAQDEKAERDELRAKLYQEEQERKE----RQKEREEAEKKARQRQEL----QQAREEQIELKERRLAEEAE 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 552 -ARVEELLMKRKEQEA-RIEQQRQEKEKAREDAARERARDREERLAAL-TAAQQEAMEELQKKIQLkhDESIRRHMEQIE 628
Cdd:pfam13868 258 rEEEEFERMLRKQAEDeEIEQEEAEKRRMKRLEHRRELEKQIEEREEQrAAEREEELEEGERLREE--EAERRERIEEER 335
|
...
gi 1211848747 629 QRK 631
Cdd:pfam13868 336 QKK 338
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
403-577 |
8.95e-06 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 50.21 E-value: 8.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 403 KRTIAESKKKHEEKQMKAQQLREKLrEEKTLKLQKLLereKDVRKWKEELLDQRRRM--MEEKLLHaefKREVQLQAIVK 480
Cdd:PRK00409 508 KKLIGEDKEKLNELIASLEELEREL-EQKAEEAEALL---KEAEKLKEELEEKKEKLqeEEDKLLE---EAEKEAQQAIK 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 481 KAQEEEAKVneIAFINTLEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKR-------------ALE 547
Cdd:PRK00409 581 EAKKEADEI--IKELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELKVGDEvkylslgqkgevlSIP 658
|
170 180 190
....*....|....*....|....*....|
gi 1211848747 548 AERQARVEELLMKRKEQEARIEQQRQEKEK 577
Cdd:PRK00409 659 DDKEAIVQAGIMKMKVPLSDLEKIQKPKKK 688
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
401-577 |
2.05e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 401 SRKRTIAESKKKHEEKQMKAQQLREKLR------EEKTLKLQKLLEREKDV-------------RKWKEELLDQRRRMme 461
Cdd:PRK03918 235 ELKEEIEELEKELESLEGSKRKLEEKIReleeriEELKKEIEELEEKVKELkelkekaeeyiklSEFYEEYLDELREI-- 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 462 EKLLHaefKREVQLQAIVKKAQEEEAKVNEIAFINTLEAQNKRHdvLSKLKEYEQRLNELQEERQRRQEEKQAR-DEAVQ 540
Cdd:PRK03918 313 EKRLS---RLEEEINGIEERIKELEEKEERLEELKKKLKELEKR--LEELEERHELYEEAKAKKEELERLKKRLtGLTPE 387
|
170 180 190
....*....|....*....|....*....|....*....
gi 1211848747 541 ERKRALEAERQAR--VEELLMKRKEQEARIEQQRQEKEK 577
Cdd:PRK03918 388 KLEKELEELEKAKeeIEEEISKITARIGELKKEIKELKK 426
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
410-613 |
2.97e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 47.61 E-value: 2.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 410 KKKHEEKQMKAQQLREKLREEKTLKLQKLLEREKDVRKWKEELLDqrRRMMEEkllHAEFKREVQLQAIVKKAQEEEakv 489
Cdd:pfam13868 164 KAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRA--KLYQEE---QERKERQKEREEAEKKARQRQ--- 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 490 nEIAFINTLEAQNKRHdVLSKLKEYEQRLNElqeerqrrqeeKQARDEAVQERKRALEAERQArveellMKRKEQEARIE 569
Cdd:pfam13868 236 -ELQQAREEQIELKER-RLAEEAEREEEEFE-----------RMLRKQAEDEEIEQEEAEKRR------MKRLEHRRELE 296
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1211848747 570 QQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQ 613
Cdd:pfam13868 297 KQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKKLK 340
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
426-641 |
3.80e-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: 48.43 E-value: 3.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 426 KLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKllhAEFKREVQLQAIVKKAQEEEAKVNEIAF--------INT 497
Cdd:pfam02463 169 RKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQA---KKALEYYQLKEKLELEEEYLLYLDYLKLneeridllQEL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 498 LEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAE-----RQARVEELLMKRKEQEARIEQQR 572
Cdd:pfam02463 246 LRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEElkselLKLERRKVDDEEKLKESEKEKKK 325
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1211848747 573 QEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLkhdESIRRHMEQIEQRKEKAAELSSGR 641
Cdd:pfam02463 326 AEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEK---LEQLEEELLAKKKLESERLSSAAK 391
|
|
| ZnF_U1 |
smart00451 |
U1-like zinc finger; Family of C2H2-type zinc fingers, present in matrin, U1 small nuclear ... |
656-688 |
4.72e-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: 4.72e-05
10 20 30
....*....|....*....|....*....|...
gi 1211848747 656 RKKQCSLCNVLISSEVYLFSHVKGRKHQQAVRE 688
Cdd:smart00451 2 GGFYCKLCNVTFTDEISVEAHLKGKKHKKNVKK 34
|
|
| Stathmin |
pfam00836 |
Stathmin family; The Stathmin family of proteins play an important role in the regulation of ... |
386-492 |
6.03e-05 |
|
Stathmin family; The Stathmin family of proteins play an important role in the regulation of the microtubule cytoskeleton. They regulate microtubule dynamics by promoting depolymerization of microtubules and/or preventing polymerization of tubulin heterodimers.
Pssm-ID: 459956 [Multi-domain] Cd Length: 136 Bit Score: 44.26 E-value: 6.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 386 PPGHGIHMHEKLSSPSRKRTIAESKkkheEKQMKAQQLREKLREEKTLK-LQKLLEREKDVRKWKEELLDQRRRMMEEKL 464
Cdd:pfam00836 23 PPSVNAAPPKLSLSPKKKDSSLEEI----QKKLEAAEERRKSLEAQKLKqLAEKREKEEEALQKADEENNNFSKMAEEKL 98
|
90 100 110
....*....|....*....|....*....|..
gi 1211848747 465 LHA----EFKREVQLQAIVKKAQEEEAKVNEI 492
Cdd:pfam00836 99 KQKmeayKENREAQIAALKEKLKEKEKHVEEV 130
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
395-637 |
6.10e-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: 47.66 E-value: 6.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 395 EKLSSPSRKRTIAESKKKHEEKQMKAQQlREKLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQ 474
Cdd:pfam02463 301 ELLKLERRKVDDEEKLKESEKEKKKAEK-ELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKK 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 475 LQAIVKKAQEEEAKVNEIAFINTLEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQARV 554
Cdd:pfam02463 380 KLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELK 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 555 EELLMKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIRRHMEQIEQRKEKA 634
Cdd:pfam02463 460 LLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVE 539
|
...
gi 1211848747 635 AEL 637
Cdd:pfam02463 540 NYK 542
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
360-651 |
6.75e-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: 46.57 E-value: 6.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 360 LADYEARESWRQNTSWGDIVEEEPARPpghgihmHEKLSspsRKRTIAESKKKHEEKQMKAQQ-LREKLREEKTLKLQKL 438
Cdd:pfam15558 81 RADRREKQVIEKESRWREQAEDQENQR-------QEKLE---RARQEAEQRKQCQEQRLKEKEeELQALREQNSLQLQER 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 439 LEREKDVRKWKEELLDQRRRM--MEEKLLHAEFKREVQLQAivkKAQEEEAKvneiafiNTLE-----AQNKRHDVLskl 511
Cdd:pfam15558 151 LEEACHKRQLKEREEQKKVQEnnLSELLNHQARKVLVDCQA---KAEELLRR-------LSLEqslqrSQENYEQLV--- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 512 keyEQRLNELQEerqrrqeekQARDEAVQERK---RALEAERQaRVEELLMKRKEQEARIEQQRQEKEKAREdaarerar 588
Cdd:pfam15558 218 ---EERHRELRE---------KAQKEEEQFQRakwRAEEKEEE-RQEHKEALAELADRKIQQARQVAHKTVQ-------- 276
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1211848747 589 DREERLAALTAAQQEAMEELQKKIQLKHDESIRRHMEQIEQRKEKAAELSSGRHANTDYAPKL 651
Cdd:pfam15558 277 DKAQRARELNLEREKNHHILKLKVEKEEKCHREGIKEAIKKKEQRSEQISREKEATLEEARKT 339
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
400-636 |
6.99e-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: 46.57 E-value: 6.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 400 PSRKRTIAE---SKKKHEEKQMKAQQLREKLREEKTLKLQKLLEREKDVRKWkeeLLDQRRRMMEEKLlhAEFKREVQlq 476
Cdd:pfam15558 3 PERDRKIAAlmlARHKEEQRMRELQQQAALAWEELRRRDQKRQETLERERRL---LLQQSQEQWQAEK--EQRKARLG-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 477 aivkkaQEEEAKVnEIAFINTLEAQNKRHDVLSKlKEyEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQArvEE 556
Cdd:pfam15558 76 ------REERRRA-DRREKQVIEKESRWREQAED-QE-NQRQEKLERARQEAEQRKQCQEQRLKEKEEELQALREQ--NS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 557 LLMKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQL--KHDESIRRHMEQIEQR---- 630
Cdd:pfam15558 145 LQLQERLEEACHKRQLKEREEQKKVQENNLSELLNHQARKVLVDCQAKAEELLRRLSLeqSLQRSQENYEQLVEERhrel 224
|
....*.
gi 1211848747 631 KEKAAE 636
Cdd:pfam15558 225 REKAQK 230
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
267-579 |
8.56e-05 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 46.78 E-value: 8.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 267 EKARIENEMDPSDISNSMAEVLAKKEELADRLEKANEeaiaSAIAEEEQ--LTREIEAEENNDINIETDNDsdfsasmgs 344
Cdd:pfam02029 18 ERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSG----QGGLDEEEafLDRTAKREERRQKRLQEALE--------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 345 GSVSFCGMSMDWNDVLADYEARESWRQNTSW--GDIVEEEPARPPGHGIHMHEKLSSPSRKRTIAESKKKHEEKQMKAQQ 422
Cdd:pfam02029 85 RQKEFDPTIADEKESVAERKENNEEEENSSWekEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEEEGEEEEDKSE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 423 LREKLREEKTLKLQKLLEREKDVRKWKEE---LLDQRRRMMEEKLLHAEF---------KREVQLQAIVKKAQEEEAKVN 490
Cdd:pfam02029 165 EAEEVPTENFAKEEVKDEKIKKEKKVKYEskvFLDQKRGHPEVKSQNGEEevtklkvttKRRQGGLSQSQEREEEAEVFL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 491 EIAfiNTLEAQNKRHDVLSKlKEYEQRLNELQEERQRRQEEKQARdeavQERKRALEAERQARVEEllmkRKEQEARIEQ 570
Cdd:pfam02029 245 EAE--QKLEELRRRRQEKES-EEFEKLRQKQQEAELELEELKKKR----EERRKLLEEEEQRRKQE----EAERKLREEE 313
|
....*....
gi 1211848747 571 qrqEKEKAR 579
Cdd:pfam02029 314 ---EKRRMK 319
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
395-577 |
8.82e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 8.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 395 EKLSSPS-RKRTIAESKKKHEEKQMKAQQLREKLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMmeekllhaefKREV 473
Cdd:COG4717 56 DELFKPQgRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL----------EKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 474 QLQAIVKKAQEEEAKVNEIAfintleaqnkrhDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQAR 553
Cdd:COG4717 126 QLLPLYQELEALEAELAELP------------ERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEE 193
|
170 180
....*....|....*....|....
gi 1211848747 554 VEELLMKRKEQEARIEQQRQEKEK 577
Cdd:COG4717 194 LQDLAEELEELQQRLAELEEELEE 217
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
458-636 |
9.37e-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: 46.07 E-value: 9.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 458 RMMEEKLLHAEFKREVQLQAIVKKAQEEEAKvneiafintleAQNKRHDVLSKlkeyEQRLNELQEERQRRQEEKQARDE 537
Cdd:pfam13868 9 RELNSKLLAAKCNKERDAQIAEKKRIKAEEK-----------EEERRLDEMME----EERERALEEEEEKEEERKEERKR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 538 AVQERKRALEAERQARVEELLMKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTA-AQQEAMEELQKKIQLKH 616
Cdd:pfam13868 74 YRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFnEEQAEWKELEKEEEREE 153
|
170 180
....*....|....*....|
gi 1211848747 617 DESIRRHMEQIEQRKEKAAE 636
Cdd:pfam13868 154 DERILEYLKEKAEREEEREA 173
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
410-638 |
1.88e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 46.12 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 410 KKKHEEKQMKAQQLREKLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQLQAIVKKAQEEEAKV 489
Cdd:TIGR00618 657 QERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAA 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 490 NEIAFINTL-EAQNKRHDVLSKLKEYEQRLNELQEERQRrqeekqaRDEAVQERKRALEAERQARvEELLMKRKEQEARI 568
Cdd:TIGR00618 737 REDALNQSLkELMHQARTVLKARTEAHFNNNEEVTAALQ-------TGAELSHLAAEIQFFNRLR-EEDTHLLKTLEAEI 808
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1211848747 569 EQQRQEKEKAREDAARERARDRE---ERLAALTAAQQEAmeelqkKIQLKHDESIRRHMEQIEQRKEKAAELS 638
Cdd:TIGR00618 809 GQEIPSDEDILNLQCETLVQEEEqflSRLEEKSATLGEI------THQLLKYEECSKQLAQLTQEQAKIIQLS 875
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
364-637 |
2.94e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 44.86 E-value: 2.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 364 EARESWRQntswgdivEEEPARPPGHGIHMHEKLSSPSRKRTIAESKKKHEEKQMKAQQLReKLREEKTLKLQKLLEREK 443
Cdd:pfam02029 17 EERRRQKE--------EEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTA-KREERRQKRLQEALERQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 444 D----VRKWKEELLDQRRRMMEEKLLHAEFKREVQlqaivkkAQEEEAKVNEIAFINTLEAQNKRHDVLSKLKEYEQRLN 519
Cdd:pfam02029 88 EfdptIADEKESVAERKENNEEEENSSWEKEEKRD-------SRLGRYKEEETEIREKEYQENKWSTEVRQAEEEGEEEE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 520 ELQEERQRRQEEKQARDEAVQERKRALEAERQARVEELLMKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTA 599
Cdd:pfam02029 161 DKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEA 240
|
250 260 270
....*....|....*....|....*....|....*....
gi 1211848747 600 AQQEAMEELQKKIQLKHDESIRRHMEQIEQRK-EKAAEL 637
Cdd:pfam02029 241 EVFLEAEQKLEELRRRRQEKESEEFEKLRQKQqEAELEL 279
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
419-639 |
3.18e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.03 E-value: 3.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 419 KAQQLREKLREEKtlklQKLLEREKDVRKWKEELLDQRRRmmEEKLLHA----EFKREVQLQAIVKKAQEEEAKVNEI-A 493
Cdd:PRK02224 409 NAEDFLEELREER----DELREREAELEATLRTARERVEE--AEALLEAgkcpECGQPVEGSPHVETIEEDRERVEELeA 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 494 FINTLEAQ----NKRHDVLSKLKEYEQR----------LNELQEERQRRQEEKQARDEAVQERKRALEAERQARVEELLM 559
Cdd:PRK02224 483 ELEDLEEEveevEERLERAEDLVEAEDRierleerredLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAE 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 560 KRKE-QEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIRRhmEQIEQRKEKAAELS 638
Cdd:PRK02224 563 AEEEaEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERR--ERLAEKRERKRELE 640
|
.
gi 1211848747 639 S 639
Cdd:PRK02224 641 A 641
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
402-658 |
3.55e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 3.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 402 RKRTIAESKKKHEEKQMKAQQLRE---------KLREEKTLKLQKLLEREKDVRKWKEELLDQRRRM-----MEEKL--- 464
Cdd:PRK03918 264 LEERIEELKKEIEELEEKVKELKElkekaeeyiKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIkeleeKEERLeel 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 465 --LHAEFKREV-QLQAIVKKAQEEEAKVNEIAFINTLEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQE 541
Cdd:PRK03918 344 kkKLKELEKRLeELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKE 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 542 RKRALEAERQAR-------------------------VEELLMKRKEQEARIEQQRQEKEKAREDAARERARDREERLAa 596
Cdd:PRK03918 424 LKKAIEELKKAKgkcpvcgrelteehrkelleeytaeLKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELA- 502
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1211848747 597 ltaaqqEAMEELQKKIQLKHDESIRRHMEQIEQRKEKAAELSSGRHANTDYAPKLTPYERKK 658
Cdd:PRK03918 503 ------EQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKL 558
|
|
| zf-met |
pfam12874 |
Zinc-finger of C2H2 type; This is a zinc-finger domain with the CxxCx(12)Hx(6)H motif, found ... |
660-682 |
3.90e-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: 3.90e-04
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
397-630 |
4.03e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 4.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 397 LSSPSRKRTIAESK---KKHEEKQMKAQQLREKLREEKTlKLQKLLEREKDVRKWKEeLLDQRRRMmEEKLlhaefkREV 473
Cdd:PRK03918 445 LTEEHRKELLEEYTaelKRIEKELKEIEEKERKLRKELR-ELEKVLKKESELIKLKE-LAEQLKEL-EEKL------KKY 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 474 QLQAIVKKAQEEEaKVNEIAfiNTLEAQnkrhdvLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQAR 553
Cdd:PRK03918 516 NLEELEKKAEEYE-KLKEKL--IKLKGE------IKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFES 586
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 554 VEELLMKRKE---------------QEARIEQQRQEKEKAREDAARERARDREERLAALTaaqqEAMEELQKKIQLKHDE 618
Cdd:PRK03918 587 VEELEERLKElepfyneylelkdaeKELEREEKELKKLEEELDKAFEELAETEKRLEELR----KELEELEKKYSEEEYE 662
|
250
....*....|..
gi 1211848747 619 SIRRHMEQIEQR 630
Cdd:PRK03918 663 ELREEYLELSRE 674
|
|
| CCDC47 |
pfam07946 |
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ... |
532-615 |
4.90e-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: 4.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 532 KQARDEAVQERKRALEAERQarvEELLMKRKEQEarieqqRQEKEKaredaarerardreeRLAALTAAQQEAMEELQKK 611
Cdd:pfam07946 263 KKTREEEIEKIKKAAEEERA---EEAQEKKEEAK------KKEREE---------------KLAKLSPEEQRKYEEKERK 318
|
....
gi 1211848747 612 IQLK 615
Cdd:pfam07946 319 KEQR 322
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
532-659 |
5.42e-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: 5.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 532 KQARDEAVQERKRALEAE-RQARVEEllmKRKEQEariEQQRQEKEKAREDAARErardreerlAALTAAQQEAMEELQK 610
Cdd:pfam15709 327 KREQEKASRDRLRAERAEmRRLEVER---KRREQE---EQRRLQQEQLERAEKMR---------EELELEQQRRFEEIRL 391
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1211848747 611 KIQLKHDESIRRHMEQIEQRKEKAAELSSGRHANTDYAPKLTPYERKKQ 659
Cdd:pfam15709 392 RKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQ 440
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
420-646 |
5.78e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 43.87 E-value: 5.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 420 AQQLREKLREEKTLKlQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQLQAIVKKAQEEEAKVNeiafintLE 499
Cdd:COG3064 1 AQEALEEKAAEAAAQ-ERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAE-------LA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 500 AQNKRhdvlsKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQARVEELLmKRKEQEARIEQQRQEKEKAR 579
Cdd:COG3064 73 AEAAK-----KLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAK-RKAEEEAKRKAEEERKAAEA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1211848747 580 EDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIRRHMEQIEQRKEKAAELSSGRHANTD 646
Cdd:COG3064 147 EAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAAD 213
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
398-637 |
5.96e-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: 5.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 398 SSPSRKRTIAESKKKHEEKQmkaqqlreklREEKTLKLQKLLEREKDVR-KWKEELLDQRRRMMEEKLLHAEFKREVQlq 476
Cdd:pfam15709 297 SSPTQTFVVTGNMESEEERS----------EEDPSKALLEKREQEKASRdRLRAERAEMRRLEVERKRREQEEQRRLQ-- 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 477 aivKKAQEEEAKVNEiafinTLEAQNKRHDVLSKLKEyeQRLNElqeerqrrQEEKQARDEAVQERKRALEAERqARVEE 556
Cdd:pfam15709 365 ---QEQLERAEKMRE-----ELELEQQRRFEEIRLRK--QRLEE--------ERQRQEEEERKQRLQLQAAQER-ARQQQ 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 557 LLMKRKEQEarIEQQRQEKEKAREDAARERARDREERLAA-----LTAAQQEAMEELQKKiqLKHDESIRRHMEQIEQRK 631
Cdd:pfam15709 426 EEFRRKLQE--LQRKKQQEEAERAEAEKQRQKELEMQLAEeqkrlMEMAEEERLEYQRQK--QEAEEKARLEAEERRQKE 501
|
....*.
gi 1211848747 632 EKAAEL 637
Cdd:pfam15709 502 EEAARL 507
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
406-634 |
7.39e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.85 E-value: 7.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 406 IAESKKKHEEKQMKAQQLREK-----LREEKTLKLQKLLErekdvrkwkeelLDQRRRMMEEKLLHAEFKREvQLQAIVK 480
Cdd:COG3206 184 LPELRKELEEAEAALEEFRQKnglvdLSEEAKLLLQQLSE------------LESQLAEARAELAEAEARLA-ALRAQLG 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 481 KAQEEEAKVNEIAFINTLEAQnkRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQARVEELLMK 560
Cdd:COG3206 251 SGPDALPELLQSPVIQQLRAQ--LAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAR 328
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1211848747 561 RKEQEARIEQQRQEkekaredaarerardreerLAALTAAQQEaMEELQKKIQLKhdesiRRHMEQIEQRKEKA 634
Cdd:COG3206 329 EASLQAQLAQLEAR-------------------LAELPELEAE-LRRLEREVEVA-----RELYESLLQRLEEA 377
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
401-575 |
7.49e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 7.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 401 SRKRTIAESKKKHEEKQMKAQQLREKLREEKTlKLQKLLEREKDVRKWKEELLDQRRRMME------EKLLHAEFKRE-- 472
Cdd:PRK03918 228 KEVKELEELKEEIEELEKELESLEGSKRKLEE-KIRELEERIEELKKEIEELEEKVKELKElkekaeEYIKLSEFYEEyl 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 473 VQLQAIVKKAQEEEAKVNEI-AFINTLEAQNKRHDVLSK-LKEYEQRLNELQEERQRRQEEKQARDEAVQERKR--ALEA 548
Cdd:PRK03918 307 DELREIEKRLSRLEEEINGIeERIKELEEKEERLEELKKkLKELEKRLEELEERHELYEEAKAKKEELERLKKRltGLTP 386
|
170 180
....*....|....*....|....*...
gi 1211848747 549 ERQARVEELLMKRKEQ-EARIEQQRQEK 575
Cdd:PRK03918 387 EKLEKELEELEKAKEEiEEEISKITARI 414
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
406-604 |
7.76e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 7.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 406 IAESKKKHEEKQMKAQQLREKLR------EEKTLKLQKLLEREKDVRKWKEELldqrrrmmEEKLLHAEfKREVQLQAIV 479
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDalqaelEELNEEYNELQAELEALQAEIDKL--------QAEIAEAE-AEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 480 KK----AQEEEAKVNEIAFIntLEAQN-----KRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAER 550
Cdd:COG3883 89 GEraraLYRSGGSVSYLDVL--LGSESfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAEL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1211848747 551 QARVEELLMKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEA 604
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
413-577 |
9.53e-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: 9.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 413 HEEKQMKAQQLREKLREEKTlKLQKLLEREKDVRKwKEELLDQRRRMMEEKLLHAEFKREVQLQAivkkaqeeeakvnEI 492
Cdd:COG4913 283 LWFAQRRLELLEAELEELRA-ELARLEAELERLEA-RLDALREELDELEAQIRGNGGDRLEQLER-------------EI 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 493 AfintlEAQNKRHDVLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERqARVEELLMKRKEQEARIEQQR 572
Cdd:COG4913 348 E-----RLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEEL-EALEEALAEAEAALRDLRREL 421
|
....*
gi 1211848747 573 QEKEK 577
Cdd:COG4913 422 RELEA 426
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
402-521 |
1.00e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.39 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 402 RKRTIAESKKKHEEKQMKAQQLREKLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREV-QLQAIVK 480
Cdd:COG1196 659 GGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLeAEREELL 738
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1211848747 481 KAQEEEAKVNEIAFINTLEAQNKRHDVLSKLKEYEQRLNEL 521
Cdd:COG1196 739 EELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
414-577 |
1.04e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.87 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 414 EEKQMKAQQLREKLREEKTLKLQKLLEREKDVRKWK-EELLDQRRRMMEEKLLHAEFKREVQLQAivKKAQEEEAKVNEI 492
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERlKQLEKERLAAQEQKKQAEEAAKQAALKQ--KQAEEAAAKAAAA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 493 AFINTlEAQNKRHDVLSKLKEYEQRLNElqeerqrrqeEKQARDEAVQERKRALEAERQARVEELLMKRKEQEARIEQQR 572
Cdd:PRK09510 145 AKAKA-EAEAKRAAAAAKKAAAEAKKKA----------EAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAA 213
|
....*
gi 1211848747 573 QEKEK 577
Cdd:PRK09510 214 EAKKK 218
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
395-724 |
1.06e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 43.10 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 395 EKLSSPSRKRTIAESKKKHEEKQMKAQQLREK----LREEKTLKLQKLLEREKDVRKWKEElLDQRRRMMEEKLLHAEFK 470
Cdd:COG3064 3 EALEEKAAEAAAQERLEQAEAEKRAAAEAEQKakeeAEEERLAELEAKRQAEEEAREAKAE-AEQRAAELAAEAAKKLAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 471 REVQLQAIVKKAQEEEAKVNEiafintlEAQNKRHdvlsklkeyEQRLNELQEERQRRQEEKQARDEA-VQERKRALEAE 549
Cdd:COG3064 82 AEKAAAEAEKKAAAEKAKAAK-------EAEAAAA---------AEKAAAAAEKEKAEEAKRKAEEEAkRKAEEERKAAE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 550 RQARVEELLMKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEELQKKIQLKHDESIRRHMEQIEQ 629
Cdd:COG3064 146 AEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 630 RKEKAAELSSGRHANTDYAPKLTPYERKKQCSLCNVLISSEVYLFSHVKGRKHQQAVRENTSIQGRELSDEEVEHLSLKK 709
Cdd:COG3064 226 AAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAA 305
|
330
....*....|....*
gi 1211848747 710 YIIDIVVESTAPAEA 724
Cdd:COG3064 306 ELLGAVAAEEAVLAA 320
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
422-637 |
1.16e-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: 42.60 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 422 QLREKLREEKTLKLQKLLEREKDVRKwKEELLDQRR--RMMEEKLLHAEFKREvqlqaivkkaQEEEAKVNE-IAFINTL 498
Cdd:pfam13868 10 ELNSKLLAAKCNKERDAQIAEKKRIK-AEEKEEERRldEMMEEERERALEEEE----------EKEEERKEErKRYRQEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 499 EAQNKRHDVLsKLKEYEQRLNElqeerqrrqeeKQARDEAVQERKRALEAERQARVEELLMKRKEQEARIEQQRQEKEKA 578
Cdd:pfam13868 79 EEQIEEREQK-RQEEYEEKLQE-----------REQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELE 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1211848747 579 REDAARERARDREErlAALTAAQQEAMEELQKKIQLKHDESIRRHMEQIEQRKEKAAEL 637
Cdd:pfam13868 147 KEEEREEDERILEY--LKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAER 203
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
404-811 |
1.21e-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: 43.42 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 404 RTIAESKKKHEEKQMKAQQLREKLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQLQAIVKKAQ 483
Cdd:TIGR00618 462 QESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLE 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 484 EEEAKVNEI-------AFINTLEAQNKRHDvLSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQARVEE 556
Cdd:TIGR00618 542 TSEEDVYHQltserkqRASLKEQMQEIQQS-FSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRK 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 557 LLMKRKEQEARIE----QQRQEKEkaredaarerardreerlaaLTAAQQEAMEELQKKIQLKHDESIRRHMEQIEQRKE 632
Cdd:TIGR00618 621 LQPEQDLQDVRLHlqqcSQELALK--------------------LTALHALQLTLTQERVREHALSIRVLPKELLASRQL 680
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 633 KAAELSSGRHANTDYAPKLTPYERKKQCSLCNVLISS----EVYLFSHVKGRK-HQQAVRENTSIQG-RELSDEEVEHLS 706
Cdd:TIGR00618 681 ALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDrefnEIENASSSLGSDlAAREDALNQSLKElMHQARTVLKART 760
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 707 LkkyiIDIVVESTAPAEALKDGEERQKNKKKAkkikarmNFRAKEYESLMETKNSGSDSPYKAKLQRLAKDLLKQVQVQD 786
Cdd:TIGR00618 761 E----AHFNNNEEVTAALQTGAELSHLAAEIQ-------FFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQE 829
|
410 420
....*....|....*....|....*
gi 1211848747 787 SGSwANNKVSALDRTLGEITRILEK 811
Cdd:TIGR00618 830 EEQ-FLSRLEEKSATLGEITHQLLK 853
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
434-639 |
1.65e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.72 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 434 KLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQLQAIVKKAQEEEAKVNEIafINTLE-----AQNKRHDVL 508
Cdd:PRK02224 163 KLEEYRERASDARLGVERVLSDQRGSLDQLKAQIEEKEEKDLHERLNGLESELAELDEE--IERYEeqreqARETRDEAD 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 509 SKLKEYEQRLNE----------LQEERQRRQEEKQARDEAVQERKRA---LEAERQARVEELLMKRKEQEArIEQQRQEK 575
Cdd:PRK02224 241 EVLEEHEERREEletleaeiedLRETIAETEREREELAEEVRDLRERleeLEEERDDLLAEAGLDDADAEA-VEARREEL 319
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1211848747 576 EKAREDAARErardreerLAALTAAQQEAMEELQKkiqlkHDESIRRHMEQIEQRKEKAAELSS 639
Cdd:PRK02224 320 EDRDEELRDR--------LEECRVAAQAHNEEAES-----LREDADDLEERAEELREEAAELES 370
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
415-643 |
2.54e-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: 41.44 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 415 EKQMKAQQLREKLREEKTLKLQKLLEREkDVRKWKEELLDQRRRMMEEKLLHAEFKREVQLQAIvKKAQEEEAKVNEIAF 494
Cdd:pfam13868 25 DAQIAEKKRIKAEEKEEERRLDEMMEEE-RERALEEEEEKEEERKEERKRYRQELEEQIEEREQ-KRQEEYEEKLQEREQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 495 INTLEAQNKRHDvlskLKEYEQRLNElqeerqrrQEE-KQARDEAVQERKRALEAERQA------RVEELLMKRKEQEAR 567
Cdd:pfam13868 103 MDEIVERIQEED----QAEAEEKLEK--------QRQlREEIDEFNEEQAEWKELEKEEereedeRILEYLKEKAEREEE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1211848747 568 IEQQRQEKEKaredaARERARDREERLAALTAAQQEAMEEL-QKKIQLKHDESIR-RHMEQIEQRKEKAAELSSGRHA 643
Cdd:pfam13868 171 REAEREEIEE-----EKEREIARLRAQQEKAQDEKAERDELrAKLYQEEQERKERqKEREEAEKKARQRQELQQAREE 243
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
395-793 |
2.67e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 42.37 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 395 EKLSSPSRKRTIAESKKKHEEKQMKAQQLREKLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFK--RE 472
Cdd:COG5022 820 IKLQKTIKREKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSISslKL 899
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 473 VQLQ------AIVKKAQEEEAKVNEI--AFINTLEAQNKRHDV-LSKLKEYEQ--RLNELqeerqrrQEEKQARDEAVQE 541
Cdd:COG5022 900 VNLEleseiiELKKSLSSDLIENLEFktELIARLKKLLNNIDLeEGPSIEYVKlpELNKL-------HEVESKLKETSEE 972
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 542 RKRAL----EAERQARVEELLMKRKEQEArieqQRQEKEKAREDAARERARDREERLAALTAAQQEAMEE-LQKKIQLKH 616
Cdd:COG5022 973 YEDLLkkstILVREGNKANSELKNFKKEL----AELSKQYGALQESTKQLKELPVEVAELQSASKIISSEsTELSILKPL 1048
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 617 DESIRRHMEQIEQRKEKAAELSSGRhANTDYAPKLTpYERKKQCSLCNVLISSEVYLFS--HVKGRKHQQAVRENTSIQG 694
Cdd:COG5022 1049 QKLKGLLLLENNQLQARYKALKLRR-ENSLLDDKQL-YQLESTENLLKTINVKDLEVTNrnLVKPANVLQFIVAQMIKLN 1126
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 695 reLSDEEVEHLSLKKYIIDIVVESTAPAEALKDGEERQKNKKKAKKIKARMNFRAKE--YESLMETKNSGSDS------- 765
Cdd:COG5022 1127 --LLQEISKFLSQLVNTLEPVFQKLSVLQLELDGLFWEANLEALPSPPPFAALSEKRlyQSALYDEKSKLSSSevndlkn 1204
|
410 420
....*....|....*....|....*...
gi 1211848747 766 PYKAKLQRLAKDLLKQVQVQDSGSWANN 793
Cdd:COG5022 1205 ELIALFSKIFSGWPRGDKLKKLISEGWV 1232
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
422-570 |
3.16e-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: 41.80 E-value: 3.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 422 QLREKLREEKTL-----KLQKLLEREKDVRKWKEELLDQRRRMMEEKLlhAEFKREvqLQAIVKKAQEEEAKVNEIAFIN 496
Cdd:pfam07888 35 RLEECLQERAELlqaqeAANRQREKEKERYKRDREQWERQRRELESRV--AELKEE--LRQSREKHEELEEKYKELSASS 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1211848747 497 TLEAQNKrhDVLSKLK-EYEQRLNELQEERqrrqeekQARDEAVQERKRALEAERQaRVEELLMKRKEQEARIEQ 570
Cdd:pfam07888 111 EELSEEK--DALLAQRaAHEARIRELEEDI-------KTLTQRVLERETELERMKE-RAKKAGAQRKEEEAERKQ 175
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
403-521 |
3.66e-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: 40.68 E-value: 3.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 403 KRTIAESKKKHEEKQMKAQQLREKLREEKTLKLQKLLEREkdvrkwkEELLDQRRRMMEEKLLHAEFKREvQLQAIVKKA 482
Cdd:COG1579 58 EKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEALQKE-------IESLKRRISDLEDEILELMERIE-ELEEELAEL 129
|
90 100 110
....*....|....*....|....*....|....*....
gi 1211848747 483 QEEEAKVNEiafinTLEAQNKRHDvlSKLKEYEQRLNEL 521
Cdd:COG1579 130 EAELAELEA-----ELEEKKAELD--EELAELEAELEEL 161
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
402-492 |
4.38e-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: 40.73 E-value: 4.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 402 RKRTIAESKKKHEEKQMKAQQLREKLREEKTLKLQKLLEREKDVRKWKEELLDQRRRMMEEKLLHAEFKREVQLQAIVKK 481
Cdd:pfam02841 202 KEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERSYQEHVKQLIEKMEAEREQLLAEQERMLEHKLQEQEELLKEG 281
|
90
....*....|..
gi 1211848747 482 AQEE-EAKVNEI 492
Cdd:pfam02841 282 FKTEaESLQKEI 293
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
511-637 |
5.45e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 5.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 511 LKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEaERQARVEELLMKRKEQEARIEQQRQEKEKAREDAARERARDR 590
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAE-EKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1211848747 591 EERLAALTAAQQEAMEELQKKIQ--LKHDESIRRHMEQIEQRKEKAAEL 637
Cdd:COG4717 127 LLPLYQELEALEAELAELPERLEelEERLEELRELEEELEELEAELAEL 175
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
450-613 |
7.14e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.69 E-value: 7.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 450 EELLDQRRRMMEEKLL--HAEFKREVQLQAIVKKAQEEEAKVNEIAFINTLEAQNKRHDVLSKLKEYEQRLnelqeerqr 527
Cdd:COG1196 624 GRTLVAARLEAALRRAvtLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELE--------- 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 528 rqeEKQARDEAVQERKRALEAERQARVEELLMKRKEQEARIEQQRQEKEKAREDAARERARDREERLAALTAAQQEAMEE 607
Cdd:COG1196 695 ---LEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELER 771
|
....*.
gi 1211848747 608 LQKKIQ 613
Cdd:COG1196 772 LEREIE 777
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
536-640 |
7.18e-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: 39.87 E-value: 7.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 536 DEAVQERKRALEAER-QARVEELLMKR-KEQEARIEQQRQEKEKAredaarerardreerlaaltaaQQEAMEELQKKIQ 613
Cdd:cd16269 190 DQALTEKEKEIEAERaKAEAAEQERKLlEEQQRELEQKLEDQERS----------------------YEEHLRQLKEKME 247
|
90 100
....*....|....*....|....*...
gi 1211848747 614 LKHDESIRRHMEQIEQR-KEKAAELSSG 640
Cdd:cd16269 248 EERENLLKEQERALESKlKEQEALLEEG 275
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
425-637 |
7.24e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.82 E-value: 7.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 425 EKLREEktlkLQKLLEREKDVRKWKEELLDQRRRMMEEKLlHAEfkrevQLQAIVKKAQEEEAKVnEIAFINTLEAQNKR 504
Cdd:TIGR02169 173 EKALEE----LEEVEENIERLDLIIDEKRQQLERLRRERE-KAE-----RYQALLKEKREYEGYE-LLKEKEALERQKEA 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 505 HDV-LSKLKEYEQRLNELQEERQRRQEEKQARDEAVQERKRALEAERQARVEELLMKRKEQEARIEQQRQEKEKAREDAA 583
Cdd:TIGR02169 242 IERqLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAE 321
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1211848747 584 RErardrEERLAALTAAQQEAMEELQKKIQlkhDESIRRH--MEQIEQRKEKAAEL 637
Cdd:TIGR02169 322 ER-----LAKLEAEIDKLLAEIEELEREIE---EERKRRDklTEEYAELKEELEDL 369
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
441-636 |
8.67e-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: 8.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 441 REKDVRKWKeelldQRRRMM----EEKLlhAEFKREV-QLQAIVKKAQEEEAKVNEIafintLEAQNKRHDVLSKLKEY- 514
Cdd:COG4913 590 HEKDDRRRI-----RSRYVLgfdnRAKL--AALEAELaELEEELAEAEERLEALEAE-----LDALQERREALQRLAEYs 657
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 515 --EQRLNELQEERQRRQEEKQARD------EAVQERKRALEAERQA---RVEELLMKRKEQEARIEQQRQEKEKAREDAA 583
Cdd:COG4913 658 wdEIDVASAEREIAELEAELERLDassddlAALEEQLEELEAELEEleeELDELKGEIGRLEKELEQAEEELDELQDRLE 737
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1211848747 584 RERARDREERLAALTAA-QQEAMEELQKKIQlkhdESIRRHMEQIEQRKEKAAE 636
Cdd:COG4913 738 AAEDLARLELRALLEERfAAALGDAVERELR----ENLEERIDALRARLNRAEE 787
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
401-577 |
9.04e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 9.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 401 SRKRTIAESKKKHEEKQMKAQQLREKLREEKTL--KLQKLLEREKDVRKWKEEL--LDQRRRMMEE---KLLHAEfKREV 473
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERREAlqRLAEYSWDEIDVASAEREIaeLEAELERLDAssdDLAALE-EQLE 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 474 QLQAIVKKAQEEEAKVNEIAFintlEAQNKRHDVLSKLKEYEQRLNElqeerqrrqeekqARDEAVQERKRALEAERQAR 553
Cdd:COG4913 696 ELEAELEELEEELDELKGEIG----RLEKELEQAEEELDELQDRLEA-------------AEDLARLELRALLEERFAAA 758
|
170 180
....*....|....*....|....
gi 1211848747 554 VEELLMKRKEQEARIEQQRQEKEK 577
Cdd:COG4913 759 LGDAVERELRENLEERIDALRARL 782
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
533-636 |
9.99e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 39.79 E-value: 9.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1211848747 533 QARDEAVQERKRALEAERQARVEEllMKRKEQEARI--EQQRQEKEKAREDAARERARDREERLAALTAAQQeAMEELQK 610
Cdd:PRK09510 93 QQKQAAEQERLKQLEKERLAAQEQ--KKQAEEAAKQaaLKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKK-AAAEAKK 169
|
90 100
....*....|....*....|....*.
gi 1211848747 611 KiqlkhdesirrhmEQIEQRKEKAAE 636
Cdd:PRK09510 170 K-------------AEAEAAKKAAAE 182
|
|
| |
