|
Name |
Accession |
Description |
Interval |
E-value |
| C2-C2_1 |
pfam11618 |
First C2 domain of RPGR-interacting protein 1; This domain is the first, more N-terminal, C2 ... |
595-736 |
4.81e-67 |
|
First C2 domain of RPGR-interacting protein 1; This domain is the first, more N-terminal, C2 domain on X-linked retinitis pigmentosa GTPase regulator-interacting proteins, or RPGR-interacting proteins.
Pssm-ID: 463310 Cd Length: 143 Bit Score: 222.12 E-value: 4.81e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 595 TLHFERREGLFEIHISKVIFSSEAVHAFGDHEPATFCTYAFYDFELQATPVLHGHTLSYDFTSQYLAQIDDSFLHYIQSN 674
Cdd:pfam11618 1 TVELERGENLFELHIGGVTFSPEALRALGDKEPSTFCTYDFYDFETQTTPVVRGLNPFYDFTSQYKVTVDDLFLQYLQTN 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024349574 675 SVTLEVHHAYGTDYETVATCQLALHEVLEQ-NGRIYSTAVLVGINGNIQDFGTVEYWVRLQAP 736
Cdd:pfam11618 81 SLTLELHQALGVDFKTLAAAQLRLHGLLEDrGGRIHGTVTLTGVEGEIQIIGTLEYWIRLRVP 143
|
|
| RPGR1_C |
pfam18111 |
Retinitis pigmentosa G-protein regulator interacting C-terminal; This is the C-terminal domain ... |
1098-1261 |
1.13e-56 |
|
Retinitis pigmentosa G-protein regulator interacting C-terminal; This is the C-terminal domain of retinitis pigmentosa G-protein regulator (RPGR) interacting protein-1 present in Homo sapiens. A mutation in RPGR interacting protein-1 can be observed in the eye disease Leber congenital amaurosis. The domain is commonly known as the RPGR-interacting domain (RID) and is thought to have a C2-like fold.
Pssm-ID: 465655 Cd Length: 166 Bit Score: 193.40 E-value: 1.13e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 1098 ATEKIRIEIISLGLT-ESRIVEDNTIQQLFVECRLYNFIAE--ETPVSLPKPPCGQRVHYNYSNVIHVDKANNRARREYL 1174
Cdd:pfam18111 1 DSDTIRIEIISLQLLnESEVMQDDNIQQLFVEYRFLGRPEEetETPVSLPKPKTGQELYYNFSKVIDVDKEKNSARREIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 1175 KSILQKPSLRTDRLLFTVVSDPPeDEQDLECEDIGFAYVSLREIFEKKRDVIEQDIFVFDSQDDSAVIGKLRVTVEALHA 1254
Cdd:pfam18111 81 RSMLLPEDPNQGNLKFTVVSEPL-DTEDGECEEIGYAYVDLKQILQSGRDIIEQDLDVKDARDENEQIGKLKVSVEALAA 159
|
....*..
gi 2024349574 1255 LCSVYEE 1261
Cdd:pfam18111 160 LRAIYSE 166
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
198-497 |
5.60e-15 |
|
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: 80.49 E-value: 5.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 198 LEDARAKIRNLETVIDSQRGRIQELEHLSELLGSQLRNKEKEIEESALHLKEQEAARQRSNirdnVEMIKVRKQLAEKSS 277
Cdd:TIGR02168 700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE----AEIEELEERLEEAEE 775
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 278 ALAAMESKFLQLQENQRNFKTNHDVLIAKSEELNVQLKEERSKCLHLEKELQSvaiSKRRTEELEERVNDLEREKELLKE 357
Cdd:TIGR02168 776 ELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES---LERRIAATERRLEDLEEQIEELSE 852
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 358 NCDKLSSSVfsmtreqewklkeEQLKLQIAELETAIQSSLADKDEILGKLKVERDKKEKLMEENKDLQSCYLENKQQLDE 437
Cdd:TIGR02168 853 DIESLAAEI-------------EELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEE 919
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024349574 438 LKDYMKYLTKRCdvDVAELSEALLLIKVRKEQKKNGDLI--CLEKDDDDIQKVsERSMRKLQ 497
Cdd:TIGR02168 920 LREKLAQLELRL--EGLEVRIDNLQERLSEEYSLTLEEAeaLENKIEDDEEEA-RRRLKRLE 978
|
|
| C2 |
cd00030 |
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ... |
786-881 |
7.35e-13 |
|
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.
Pssm-ID: 175973 [Multi-domain] Cd Length: 102 Bit Score: 65.94 E-value: 7.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 786 LHVTIKCCNRLQSQKKHLQPNSYVVYKFFDFAHHDTRIIPSSSNPQIDDHMCFQVPMTADldqylkwESLTFYVFDDSEM 865
Cdd:cd00030 1 LRVTVIEARNLPAKDLNGKSDPYVKVSLGGKQKFKTKVVKNTLNPVWNETFEFPVLDPES-------DTLTVEVWDKDRF 73
|
90
....*....|....*.
gi 2024349574 866 GEDGFLGKANVPLIPL 881
Cdd:cd00030 74 SKDDFLGEVEIPLSEL 89
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
203-472 |
5.62e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.35 E-value: 5.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 203 AKIRNLETVIDSQRGRIQELEHLSELLGSQLRNKEKEIEESALHLKEQEAARQRSNIRDNV---EMIKVRKQLAEKSSAL 279
Cdd:COG1196 232 LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEllaELARLEQDIARLEERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 280 AAMESKFLQLQENQRNFKTNHDVLIAKSEELNVQLKEERSKCLHLEKELQSVAisKRRTEELEERVNDLEREKELLKENC 359
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE--EALLEAEAELAEAEEELEELAEELL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 360 DKLSSSVFSMTREQEWKLKEEQLKLQIAELETAIQSSLADKDEILGKLKVERDKKEKLMEENKDLQscylENKQQLDELK 439
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE----EEEEALLELL 465
|
250 260 270
....*....|....*....|....*....|...
gi 2024349574 440 DYMKYLTKRCDVDVAELSEALLLIKVRKEQKKN 472
Cdd:COG1196 466 AELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
209-543 |
6.68e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 70.47 E-value: 6.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 209 ETVIDSQRGRIQELEHLSELLGSQLRNKEKEIeesalhlkeQEAARQRSNIRDNVEmiKVRKQLAEKSSALAAMESKFLQ 288
Cdd:TIGR02168 669 NSSILERRREIEELEEKIEELEEKIAELEKAL---------AELRKELEELEEELE--QLRKELEELSRQISALRKDLAR 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 289 LQENQRNFKTNHDVLIAKSEELNVQLKEERSKclhLEKELQSVAISKRRTEELEERVNDLEREKELLKENCDKLSSSVFS 368
Cdd:TIGR02168 738 LEAEVEQLEERIAQLSKELTELEAEIEELEER---LEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 369 MTRE-QEWKLKEEQLKLQIAELETAIQssladkdEILGKLKVERDKKEKLMEENKDLQscylenkQQLDELKDYMKYLTK 447
Cdd:TIGR02168 815 LNEEaANLRERLESLERRIAATERRLE-------DLEEQIEELSEDIESLAAEIEELE-------ELIEELESELEALLN 880
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 448 RcdvdVAELSEALLLIKVRKEQKKNGdlicLEKDDDDIQKvSERSMRKLQLAHAETVQELEKTRSMLI-VQHKINKGYQT 526
Cdd:TIGR02168 881 E----RASLEEALALLRSELEELSEE----LRELESKRSE-LRRELEELREKLAQLELRLEGLEVRIDnLQERLSEEYSL 951
|
330
....*....|....*..
gi 2024349574 527 EIEAVTQKMESLQKDYE 543
Cdd:TIGR02168 952 TLEEAEALENKIEDDEE 968
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
198-476 |
1.68e-10 |
|
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: 65.85 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 198 LEDARAKIRNLETVIDSQRGRIQELEHLSELLGS---QLRNKEKEIEESALHLKEQEAARQRSNIRDNVEMIKVRKQLAE 274
Cdd:TIGR02168 255 LEELTAELQELEEKLEELRLEVSELEEEIEELQKelyALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 275 KSSALAAMESKFLQLQENQRNFKTNHDVLIAKSEELN-------VQLKEERSKCLHLEKELQSvaISKRRtEELEERVND 347
Cdd:TIGR02168 335 LAEELAELEEKLEELKEELESLEAELEELEAELEELEsrleeleEQLETLRSKVAQLELQIAS--LNNEI-ERLEARLER 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 348 LEREKELLKENcdklsssvfsmTREQEWKLKEEQLKlqiaeletAIQSSLADKDEILGKLKVERDKKEKLMEEnkdLQSC 427
Cdd:TIGR02168 412 LEDRRERLQQE-----------IEELLKKLEEAELK--------ELQAELEELEEELEELQEELERLEEALEE---LREE 469
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2024349574 428 YLENKQQLDELKDYMKYLTKRCDVDVAELSEALLLIKVRKEQKKNGDLI 476
Cdd:TIGR02168 470 LEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGL 518
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
198-426 |
5.83e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.80 E-value: 5.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 198 LEDARAKIRNLETVIDSQRGRIQELEHLSELLGSQLRNKEKEI---EESALHLKEQEAARQRSNIRDNVEMIKVRKQLAE 274
Cdd:COG1196 255 LEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELarlEQDIARLEERRRELEERLEELEEELAELEEELEE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 275 KSSALAAMESKFLQLQENQR----NFKTNHDVLIAKSEELNVQLKEERSKCLHLEKELQSVAISKRRTEELEERVNDLER 350
Cdd:COG1196 335 LEEELEELEEELEEAEEELEeaeaELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024349574 351 EKELLKENCDKLSSSVFSMTRE-QEWKLKEEQLKLQIAELETAIQSSLADKDEILGKLKVERDKKEKLMEENKDLQS 426
Cdd:COG1196 415 RLERLEEELEELEEALAELEEEeEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAA 491
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
205-570 |
6.11e-10 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 63.98 E-value: 6.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 205 IRNLETVIDSQRGRIQELEHLSELLGSQLRNK-----------------EKEIEESALHLKEQEAARQRSNIRDNVEMIK 267
Cdd:pfam15921 226 LRELDTEISYLKGRIFPVEDQLEALKSESQNKielllqqhqdrieqlisEHEVEITGLTEKASSARSQANSIQSQLEIIQ 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 268 --VRKQLAEKSSALAAMESKFLQLQENQRNFK-------------------------TNHDVLIAKSEELNVQLKE---- 316
Cdd:pfam15921 306 eqARNQNSMYMRQLSDLESTVSQLRSELREAKrmyedkieelekqlvlanseltearTERDQFSQESGNLDDQLQKllad 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 317 --ERSKCLHLEKELQ----------SVAISKRRtEELEERVNDLEREKELLKencdklsssvfSMTREQEWKLKEE---- 380
Cdd:pfam15921 386 lhKREKELSLEKEQNkrlwdrdtgnSITIDHLR-RELDDRNMEVQRLEALLK-----------AMKSECQGQMERQmaai 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 381 QLKLQIAELETAIQSSLADKDEILGKLKVERDKKEKLMEENK----DLQSCYLENKQQLDELKDYMKYLTKRCDVDVAEL 456
Cdd:pfam15921 454 QGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSErtvsDLTASLQEKERAIEATNAEITKLRSRVDLKLQEL 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 457 SEalllikvrkeqkkngdlicLEKDDDDIQKV-SERSMRKLQLAHAETVQELEKTR----SMLIVQHKINKGyqtEIEAV 531
Cdd:pfam15921 534 QH-------------------LKNEGDHLRNVqTECEALKLQMAEKDKVIEILRQQienmTQLVGQHGRTAG---AMQVE 591
|
410 420 430
....*....|....*....|....*....|....*....
gi 2024349574 532 TQKMESLQKDYELKIGKYVDLLDMKAARIKKLEAQLRDV 570
Cdd:pfam15921 592 KAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDL 630
|
|
| C2 |
pfam00168 |
C2 domain; |
786-893 |
2.39e-09 |
|
C2 domain;
Pssm-ID: 425499 [Multi-domain] Cd Length: 104 Bit Score: 55.79 E-value: 2.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 786 LHVTIKCCNRLQSQKKHLQPNSYVVYKFFDFAH-HDTRIIPSSSNPQIDDHMCFQVPMTADldqylkwESLTFYVFDDSE 864
Cdd:pfam00168 3 LTVTVIEAKNLPPKDGNGTSDPYVKVYLLDGKQkKKTKVVKNTLNPVWNETFTFSVPDPEN-------AVLEIEVYDYDR 75
|
90 100
....*....|....*....|....*....
gi 2024349574 865 MGEDGFLGKANVPLIPLACNRSISGTFEV 893
Cdd:pfam00168 76 FGRDDFIGEVRIPLSELDSGEGLDGWYPL 104
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
198-543 |
2.77e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 61.62 E-value: 2.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 198 LEDARAKIRNLETVIDSQRGRIQEL--EHLSELLGSQLRNKEKEIEESALHLKEQEAARQRSNIRdnvemikvrKQLAEK 275
Cdd:TIGR02169 179 LEEVEENIERLDLIIDEKRQQLERLrrEREKAERYQALLKEKREYEGYELLKEKEALERQKEAIE---------RQLASL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 276 SSALAAMESkflQLQENQRNFKTNHDVLiaksEELNVQLKEERS-KCLHLEKELQSVAISKRRTE----ELEERVNDLER 350
Cdd:TIGR02169 250 EEELEKLTE---EISELEKRLEEIEQLL----EELNKKIKDLGEeEQLRVKEKIGELEAEIASLErsiaEKERELEDAEE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 351 EKELLKENCDKLSSSVFSMTRE-QEWKLKEEQLKLQIAELETAIQSSLADKDEILGKLKVERDKKEKLMEENKDLQSCYL 429
Cdd:TIGR02169 323 RLAKLEAEIDKLLAEIEELEREiEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREIN 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 430 ENKQQLDELKDymkyLTKRCDVDVAELSEALllikVRKEQKKNGdlicLEKDDDDIQKVSERSMRKLQlahaETVQELEK 509
Cdd:TIGR02169 403 ELKRELDRLQE----ELQRLSEELADLNAAI----AGIEAKINE----LEEEKEDKALEIKKQEWKLE----QLAADLSK 466
|
330 340 350
....*....|....*....|....*....|....
gi 2024349574 510 TRSMLivqhkinKGYQTEIEAVTQKMESLQKDYE 543
Cdd:TIGR02169 467 YEQEL-------YDLKEEYDRVEKELSKLQRELA 493
|
|
| C2 |
smart00239 |
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ... |
786-878 |
3.02e-09 |
|
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, protein kinases C, and synaptotagmins (among others). Some do not appear to contain Ca2+-binding sites. Particular C2s appear to bind phospholipids, inositol polyphosphates, and intracellular proteins. Unusual occurrence in perforin. Synaptotagmin and PLC C2s are permuted in sequence with respect to N- and C-terminal beta strands. SMART detects C2 domains using one or both of two profiles.
Pssm-ID: 214577 [Multi-domain] Cd Length: 101 Bit Score: 55.57 E-value: 3.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 786 LHVTIKCCNRLQSQKKHLQPNSYVVYKFFDFAHHD--TRIIPSSSNPQIDDHMCFQVPMTADldqylkwESLTFYVFDDS 863
Cdd:smart00239 2 LTVKIISARNLPPKDKGGKSDPYVKVSLDGDPKEKkkTKVVKNTLNPVWNETFEFEVPPPEL-------AELEIEVYDKD 74
|
90
....*....|....*
gi 2024349574 864 EMGEDGFLGKANVPL 878
Cdd:smart00239 75 RFGRDDFIGQVTIPL 89
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
198-425 |
5.03e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 5.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 198 LEDARAKIRNLETVIDSQRG-------RIQELEHLSELLGSQLRNKEKEIEEsalhLKEQEAARQRSNIRDNVEMIKVRK 270
Cdd:COG1196 269 LEELRLELEELELELEEAQAeeyellaELARLEQDIARLEERRRELEERLEE----LEEELAELEEELEELEEELEELEE 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 271 QLAEKSSALAAMESKFLQLQENQRNFKTNHDVLIAKSEELNVQLKEERSKCLHLEKELQSVAIS----KRRTEELEERVN 346
Cdd:COG1196 345 ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAeealLERLERLEEELE 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 347 DLEREKELLKENCDKLSSSVFSMTREQ-EWKLKEEQLKLQIAELETAIQSSLADKDEILGKLKVERDKKEKLMEENKDLQ 425
Cdd:COG1196 425 ELEEALAELEEEEEEEEEALEEAAEEEaELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
99-439 |
7.64e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.47 E-value: 7.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 99 RLGRTVKMEGMVEHLQERVRDLEKQNEILRSKLISNKQQIHMPShrpIQYKFAQPRNSNGLKKASDAAGTPEPTKKgmRL 178
Cdd:TIGR02169 665 GILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELS---QELSDASRKIGEIEKEIEQLEQEEEKLKE--RL 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 179 QNLEVRspplvlrrcgpnlLEDARAKIRNLETVIDSQRGRIQELEHLSELLGSQLRNKEKEIEESALHLKEQEAARQRSN 258
Cdd:TIGR02169 740 EELEED-------------LSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEE 806
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 259 IRDNVEMIK----------VRKQLAEKSSalAAMESKFLQLQENQRNFKTNHDVLIAKSEELNVQLKEERSKCLHLEKEL 328
Cdd:TIGR02169 807 VSRIEARLReieqklnrltLEKEYLEKEI--QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRL 884
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 329 Q-------------SVAISKRRT-----EELEERVNDLEREKELLKENCDKLSSSVFSMTREQEWKLKEEQLKLQIAELE 390
Cdd:TIGR02169 885 GdlkkerdeleaqlRELERKIEEleaqiEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVE 964
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2024349574 391 TAIQS-------SLADKDEILGKLKVERDKKEKLMEENKDLqscyLENKQQLDELK 439
Cdd:TIGR02169 965 EEIRAlepvnmlAIQEYEEVLKRLDELKEKRAKLEEERKAI----LERIEEYEKKK 1016
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
198-577 |
2.74e-08 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 58.19 E-value: 2.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 198 LEDARAKIRNLETVIDSQRGRIQELEHLSELLGSQLrnkEKEIEESALHLKEQEAARQRSNIrdnvemikvrkqLAEKSS 277
Cdd:pfam05483 101 LKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKL---EEEIQENKDLIKENNATRHLCNL------------LKETCA 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 278 ALAAMESKFLQLQENQR----NFKTNHDVLIAKSEELNVQ-----------LKEERSKCLHLEKELQSVAISKRRTEEL- 341
Cdd:pfam05483 166 RSAEKTKKYEYEREETRqvymDLNNNIEKMILAFEELRVQaenarlemhfkLKEDHEKIQHLEEEYKKEINDKEKQVSLl 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 342 ----EERVNDLEREKELLKENCDKLSSsvfsmtREQEWKLKEEQLKlQIAELETAIQSSLAD-KDEILGKLKVERDKKEK 416
Cdd:pfam05483 246 liqiTEKENKMKDLTFLLEESRDKANQ------LEEKTKLQDENLK-ELIEKKDHLTKELEDiKMSLQRSMSTQKALEED 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 417 LMEENKDLQSCYLENKQQLDEL---KDYMKYLTKRCDVDVAELSEALllikvRKEQKKngdlicLEKDDDDIQKVSERSM 493
Cdd:pfam05483 319 LQIATKTICQLTEEKEAQMEELnkaKAAHSFVVTEFEATTCSLEELL-----RTEQQR------LEKNEDQLKIITMELQ 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 494 RKlqLAHAETVQELEKTRSMLIVQHKINKGYQTEIEAVTQKMESLQKDYELKIGKYVDLLDMKAARIKKLEAQLRDVAYG 573
Cdd:pfam05483 388 KK--SSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTS 465
|
....
gi 2024349574 574 SKRY 577
Cdd:pfam05483 466 EEHY 469
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
198-531 |
1.86e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.71 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 198 LEDARAKIRNLETVIDSQRGRIQELEH----------LSELLgsqlrnKEKEIEESALHLK--EQEAARQRSNIRDNVEM 265
Cdd:COG1196 181 LEATEENLERLEDILGELERQLEPLERqaekaeryreLKEEL------KELEAELLLLKLRelEAELEELEAELEELEAE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 266 IKV-RKQLAEKSSALAAMESKFLQLQENQRNFKTNHDVLIAKSEELNVQLKEERSKCLHLEKELQSVAiskRRTEELEER 344
Cdd:COG1196 255 LEElEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELE---EELAELEEE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 345 VNDLEREKELLKENCDKLsssvfsmtrEQEWKLKEEQLKLQIAELETAIQSSLADKDEILGKLKVERDKKEKLMEENKDL 424
Cdd:COG1196 332 LEELEEELEELEEELEEA---------EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 425 QSCYLENKQQLDELKDYMKYLTKRCDVDVAELSEAL-LLIKVRKEQKKNGDLICLEKDDDDIQKVSERSMRKLQLAHAET 503
Cdd:COG1196 403 EELEEAEEALLERLERLEEELEELEEALAELEEEEEeEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482
|
330 340
....*....|....*....|....*...
gi 2024349574 504 VQELEKTRSMLIVQHKINKGYQTEIEAV 531
Cdd:COG1196 483 LEELAEAAARLLLLLEAEADYEGFLEGV 510
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
198-570 |
1.98e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.46 E-value: 1.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 198 LEDARAKIRNLETVIDSQRGRIQELEHL---SELLGSQLRNKEKEIEE-----SALHLKEQEAARQRSNIRDNVEMIK-- 267
Cdd:PRK03918 157 LDDYENAYKNLGEVIKEIKRRIERLEKFikrTENIEELIKEKEKELEEvlreiNEISSELPELREELEKLEKEVKELEel 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 268 ------VRKQLAEKSSALAAMESKFLQLQENQRNFKTNHDVL---------IAKSEELNVQLKEERSKCL----HLEKEL 328
Cdd:PRK03918 237 keeieeLEKELESLEGSKRKLEEKIRELEERIEELKKEIEELeekvkelkeLKEKAEEYIKLSEFYEEYLdelrEIEKRL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 329 QSVaisKRRTEELEERVNDLEREKELLKENCDKLSSSVFSMTREQEWKLKEEQLKLQIAELETaIQSSLADK--DEILGK 406
Cdd:PRK03918 317 SRL---EEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELER-LKKRLTGLtpEKLEKE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 407 LKVERDKKEKLMEENKDLQSCYLENKQQLDELKDYMKYLTK---RCDVDVAELSEalllikvrkEQKKNgdliCLEKDDD 483
Cdd:PRK03918 393 LEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgKCPVCGRELTE---------EHRKE----LLEEYTA 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 484 DIQKVSERsMRKLQLAHAETVQELEKTRSMLIVQHKINKGYQT--EIEAVTQKM-----ESLQKDYE---------LKIG 547
Cdd:PRK03918 460 ELKRIEKE-LKEIEEKERKLRKELRELEKVLKKESELIKLKELaeQLKELEEKLkkynlEELEKKAEeyeklkeklIKLK 538
|
410 420
....*....|....*....|...
gi 2024349574 548 KYVDLLDMKAARIKKLEAQLRDV 570
Cdd:PRK03918 539 GEIKSLKKELEKLEELKKKLAEL 561
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
195-420 |
2.37e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.38 E-value: 2.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 195 PNLLEDARAKIRNLETVIDSQRGRIQELEHLSELLGSQLRNKEKEIEESA--LHLKEQEAARQRSNIRDN-VEMIKVRKQ 271
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALArrIRALEQELAALEAELAELeKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 272 LAEKSSALAAMeskflqLQENQRNFKTNHDVLIAKSEELNvqlkeERSKCLHLEKELqsVAISKRRTEELEERVNDLERE 351
Cdd:COG4942 99 LEAQKEELAEL------LRALYRLGRQPPLALLLSPEDFL-----DAVRRLQYLKYL--APARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024349574 352 KELLKENCDKLSSsvfSMTREQEWKLKEEQLKLQIAELETAIQSSLADKDEILGKLKVERDKKEKLMEE 420
Cdd:COG4942 166 RAELEAERAELEA---LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
198-569 |
2.43e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.43 E-value: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 198 LEDARAKIRNLETVIDSQRGRIQELEHlsellgsqlRNKEKEIEESALHLKEQEAARQRSNIRDNVEMIkvRKQLAEKSS 277
Cdd:PRK02224 330 LEECRVAAQAHNEEAESLREDADDLEE---------RAEELREEAAELESELEEAREAVEDRREEIEEL--EEEIEELRE 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 278 ALAAMESKFLQLQENQRNFKTNHDVLIAKSEELNVQLKEERS------------KCLHLEKELQ------SVAISKRRTE 339
Cdd:PRK02224 399 RFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARErveeaealleagKCPECGQPVEgsphveTIEEDRERVE 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 340 ELEERVNDLEREKELLKENCDKLSSSVFSMTREQEWKLKEEQLKLQIAELET-------AIQSSLADKDEILGKLKVERD 412
Cdd:PRK02224 479 ELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERREtieekreRAEELRERAAELEAEAEEKRE 558
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 413 KKEKLMEENKDLQSCYLENKQQLDELKDYMKYLTKRCDVdVAELSEALLLIKVRKEQKKNGDliclEKDDDDIQKVSERS 492
Cdd:PRK02224 559 AAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTL-LAAIADAEDEIERLREKREALA----ELNDERRERLAEKR 633
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024349574 493 MRKLQLAHAETVQELEKTRSmlivQHKINKGYQTEIEAVTQKMESLQKDYELKIGkyvdlldMKAARIKKLEAqLRD 569
Cdd:PRK02224 634 ERKRELEAEFDEARIEEARE----DKERAEEYLEQVEEKLDELREERDDLQAEIG-------AVENELEELEE-LRE 698
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
204-564 |
4.09e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 54.64 E-value: 4.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 204 KIRNLETVIDSQRGRIQELEHLSELLGSQLRNKEKEIEESALHLKEQEAarQRSNIRDNVEMIKvrkqlAEKSSALAAME 283
Cdd:TIGR04523 240 EINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEK--QLNQLKSEISDLN-----NQKEQDWNKEL 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 284 SKFLQLQENQrnfKTNHDVLIAKSEELNVQLKEERSKclhLEKELQ-SVAISKRRTEELEERVNDLEREKellKENcdkl 362
Cdd:TIGR04523 313 KSELKNQEKK---LEEIQNQISQNNKIISQLNEQISQ---LKKELTnSESENSEKQRELEEKQNEIEKLK---KEN---- 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 363 sssvfsmtreQEWKLKEEQLKLQIAELETAIQSSLADKDEILGKLKVERDKKEKLMEENKDLQSCYLENKQQLDELKD-- 440
Cdd:TIGR04523 380 ----------QSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNqd 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 441 -----YMKYLTKRCDVDVAELSEALLLIK-VRKEQKKNGDLIclekdDDDIQKVSERSMRKLQLahAETVQELEKTRSML 514
Cdd:TIGR04523 450 svkelIIKNLDNTRESLETQLKVLSRSINkIKQNLEQKQKEL-----KSKEKELKKLNEEKKEL--EEKVKDLTKKISSL 522
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2024349574 515 IVQHKINKGYQTEIEAVTQKMES--LQKDYELKIGKYVDLLDMKAARIKKLE 564
Cdd:TIGR04523 523 KEKIEKLESEKKEKESKISDLEDelNKDDFELKKENLEKEIDEKNKEIEELK 574
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
232-556 |
7.71e-07 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 53.82 E-value: 7.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 232 QLRNKEKEIEESALHLKEQEAARQRS-NIRDNVEMIKVRKQLAEKSSALAAMESKFLQLQENQRNFKTNHDVLIAKSEEL 310
Cdd:pfam02463 187 ELIIDLEELKLQELKLKEQAKKALEYyQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEK 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 311 NVQLKEERSKC---LHLEKELQSVAISKRRTEE-----LEERVNDLEREKELLKENCDKLSSSvfsmtrEQEWKLKEEQL 382
Cdd:pfam02463 267 LAQVLKENKEEekeKKLQEEELKLLAKEEEELKsellkLERRKVDDEEKLKESEKEKKKAEKE------LKKEKEEIEEL 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 383 KLQIAELETAIQSSLADKDEILGKLKVERDKKEKLMEENKDLQScYLENKQQLDELKDYMKYLTKRCDVDVAELSEALLL 462
Cdd:pfam02463 341 EKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESE-RLSSAAKLKEEELELKSEEEKEAQLLLELARQLED 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 463 IKVRKEQKKNGDLICLEKDDDDIQ-KVSERSMRKLQLAHAETVQELEKTRSMLIVQHKIN---KGYQTEIEAVTQKMESL 538
Cdd:pfam02463 420 LLKEEKKEELEILEEEEESIELKQgKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLvklQEQLELLLSRQKLEERS 499
|
330
....*....|....*...
gi 2024349574 539 QKDYELKIGKYVDLLDMK 556
Cdd:pfam02463 500 QKESKARSGLKVLLALIK 517
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
202-546 |
8.30e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 53.57 E-value: 8.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 202 RAKIRNLETVIDSQRGRIQELEHLSELLGSQLRNKEKEIEESALHLKEQEaarqrsnirdnVEMIKVRKQLAEKSSALaa 281
Cdd:pfam05483 355 EATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKE-----------VELEELKKILAEDEKLL-- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 282 meskflqlqENQRNFKTNHDVLIAKSEELNVQLKEERSKCLHLEKELQSVAISKRR-TEELEERVNDLEREK---ELLKE 357
Cdd:pfam05483 422 ---------DEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHyLKEVEDLKTELEKEKlknIELTA 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 358 NCDKLSSSVFSMTREQEwklkeeQLKLQIAELETAIQSSLADKDEILGKLKVERDKKEKLMEEnkdLQSCYLENKQQLDE 437
Cdd:pfam05483 493 HCDKLLLENKELTQEAS------DMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDE---LESVREEFIQKGDE 563
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 438 LKdymkyltkrCDVDVAELSEALLLIKVRKEQKKngdLICLEKDDDDIQKVSERSMRKLQLAHAETvQELEK-----TRS 512
Cdd:pfam05483 564 VK---------CKLDKSEENARSIEYEVLKKEKQ---MKILENKCNNLKKQIENKNKNIEELHQEN-KALKKkgsaeNKQ 630
|
330 340 350
....*....|....*....|....*....|....
gi 2024349574 513 MLIVQHKINKgYQTEIEAVTQKMESLQKDYELKI 546
Cdd:pfam05483 631 LNAYEIKVNK-LELELASAKQKFEEIIDNYQKEI 663
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
44-439 |
1.39e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.76 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 44 SRKELEDKYLQLRDENISLKQHANKQEETIKRM------ATRLIQLVHDK-KRNEQVGGGPKRLGRtvkMEGMVEHLQER 116
Cdd:PRK03918 253 SKRKLEEKIRELEERIEELKKEIEELEEKVKELkelkekAEEYIKLSEFYeEYLDELREIEKRLSR---LEEEINGIEER 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 117 VRDLEKQNEIL-----RSKLISNKQQIHMPSHRPIQYKFAQPRNSNGLKKaSDAAGTPEPTKKgmRLQNLEVRSPPLVLR 191
Cdd:PRK03918 330 IKELEEKEERLeelkkKLKELEKRLEELEERHELYEEAKAKKEELERLKK-RLTGLTPEKLEK--ELEELEKAKEEIEEE 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 192 rcgpnlLEDARAKIRNLETVIDSQRGRIQEL----------------EHLSELLGS---QLRNKEKEIEESALHLKEQEA 252
Cdd:PRK03918 407 ------ISKITARIGELKKEIKELKKAIEELkkakgkcpvcgrelteEHRKELLEEytaELKRIEKELKEIEEKERKLRK 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 253 -ARQRSNIRDNVEMIKVRKQLAEKssaLAAMESKF--LQLQENQRNFKtnhdvliaKSEELNVQLKEERSKCLHLEKELQ 329
Cdd:PRK03918 481 eLRELEKVLKKESELIKLKELAEQ---LKELEEKLkkYNLEELEKKAE--------EYEKLKEKLIKLKGEIKSLKKELE 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 330 SVAISKRRTEELEERVNDLEREKELLKencDKLSSSVFSMTREQEWKLKE-EQLKLQIAELETAiQSSLADKDEILGKLK 408
Cdd:PRK03918 550 KLEELKKKLAELEKKLDELEEELAELL---KELEELGFESVEELEERLKElEPFYNEYLELKDA-EKELEREEKELKKLE 625
|
410 420 430
....*....|....*....|....*....|..
gi 2024349574 409 VERDKK-EKLMEENKDLQscylENKQQLDELK 439
Cdd:PRK03918 626 EELDKAfEELAETEKRLE----ELRKELEELE 653
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
188-447 |
1.85e-06 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 52.52 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 188 LVLRRCGPNLLEDARAKirnlETVIDSQRGRIQELEHLSE-------LLGSQLRNKEKEIEEsalhLKEQEAARQRSNIR 260
Cdd:pfam10174 397 NVLQKKIENLQEQLRDK----DKQLAGLKERVKSLQTDSSntdtaltTLEEALSEKERIIER----LKEQREREDRERLE 468
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 261 DNVEMIKVRKQLAEKSSALAA----MESKFLQLQENQRNFKTNHDVLIAKSEELNVQLKEERSKCLHLEKEL---QSVAI 333
Cdd:pfam10174 469 ELESLKKENKDLKEKVSALQPelteKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLkkaHNAEE 548
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 334 SKRRTEELEERVNDLEREKELLKENCDKLSSSV---FSMTREQEwklKEEQLKLQ-IAELETAIQSSLADKDEILGKLK- 408
Cdd:pfam10174 549 AVRTNPEINDRIRLLEQEVARYKEESGKAQAEVerlLGILREVE---NEKNDKDKkIAELESLTLRQMKEQNKKVANIKh 625
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2024349574 409 ---VERDKKEKLMEENKDLQSCYLENKQQLdELKDYMKYLTK 447
Cdd:pfam10174 626 gqqEMKKKGAQLLEEARRREDNLADNSQQL-QLEELMGALEK 666
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
47-471 |
2.34e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.94 E-value: 2.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 47 ELEDKYLQLRDENISLKQHANKQEETIKRMATRLIQLVHDKKRN-EQVGGGPKRLGRTVK----MEGMVEHLQERVRDLE 121
Cdd:TIGR04523 222 ELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIkKQLSEKQKELEQNNKkikeLEKQLNQLKSEISDLN 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 122 KQ-----NEILRSKLISNKQQIhmpshRPIQYKFAQprNSNGLKKASDAAGTPEPTKKGMRLQNLEVRSPPLVLRRCGPN 196
Cdd:TIGR04523 302 NQkeqdwNKELKSELKNQEKKL-----EEIQNQISQ--NNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEK 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 197 LLEDARAK---IRNLETVIDSQRGRIQELEHLSELLGSQLRNKEKEIEesalhLKEQEAARQRSNIRDNVEMIK-VRKQL 272
Cdd:TIGR04523 375 LKKENQSYkqeIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKE-----LLEKEIERLKETIIKNNSEIKdLTNQD 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 273 AEKSSALAAMESKFLQLQENQRNFKTNHDVLIAKSEELNVQLKEERSKCLHLEKElqsvaiskrrTEELEERVNDLEREK 352
Cdd:TIGR04523 450 SVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEE----------KKELEEKVKDLTKKI 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 353 ELLKENCDKLSSsvfsmtreqewklKEEQLKLQIAELETAIQSSLADKD-EILGKLKVERDKK-EKLMEENKDLQSCYLE 430
Cdd:TIGR04523 520 SSLKEKIEKLES-------------EKKEKESKISDLEDELNKDDFELKkENLEKEIDEKNKEiEELKQTQKSLKKKQEE 586
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2024349574 431 NKQQLDELKDYMKYLTKRC---DVDVAELSEALLLIKvrKEQKK 471
Cdd:TIGR04523 587 KQELIDQKEKEKKDLIKEIeekEKKISSLEKELEKAK--KENEK 628
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
267-541 |
4.40e-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: 51.21 E-value: 4.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 267 KVRKQLAEKssalaameskflQLQENQRNFKTNHDVLiaksEELNVQLKeerskclHLEKELQSVAISKRRTEELEE--- 343
Cdd:TIGR02168 171 KERRKETER------------KLERTRENLDRLEDIL----NELERQLK-------SLERQAEKAERYKELKAELRElel 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 344 -----RVNDLEREKELLKENCDKLSSSVFSMTRE-QEWKLKEEQLKLQIAELETAI-------QSSLADKDEILGKLKVE 410
Cdd:TIGR02168 228 allvlRLEELREELEELQEELKEAEEELEELTAElQELEEKLEELRLEVSELEEEIeelqkelYALANEISRLEQQKQIL 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 411 RDKKEKLMEENKDLQSCYLENKQQLDELKDYMKYLTKRCDVDVAELSEALLLIKVRKEQKKNGDLICLEKDDDDIQKVSE 490
Cdd:TIGR02168 308 RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK 387
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2024349574 491 RSMRKLQLA-HAETVQELEKTRSMLIVQHKINkgyQTEIEAVTQKMESLQKD 541
Cdd:TIGR02168 388 VAQLELQIAsLNNEIERLEARLERLEDRRERL---QQEIEELLKKLEEAELK 436
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
197-549 |
4.86e-06 |
|
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: 50.89 E-value: 4.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 197 LLEDARAKIRNLE---TVIDSQRGRIQELEHLSELLGSQLR---NKEKEIEEsalhLKEQEAARQRSNIRdnvemikvRK 270
Cdd:pfam17380 301 LRQEKEEKAREVErrrKLEEAEKARQAEMDRQAAIYAEQERmamERERELER----IRQEERKRELERIR--------QE 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 271 QLAEKSSALAAMESkfLQLQENQRNFKTNHDVLIAKSEELnvqLKEERSKCLHlEKELQSVAISKRRTEELEERVNDLER 350
Cdd:pfam17380 369 EIAMEISRMRELER--LQMERQQKNERVRQELEAARKVKI---LEEERQRKIQ-QQKVEMEQIRAEQEEARQREVRRLEE 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 351 EKEllkencdklsssvfsmtREQEwKLKEEQLKLQiAELETAIQSSLADKDEILGKLKVERDKKEKLMEENKDLQSCYLE 430
Cdd:pfam17380 443 ERA-----------------REME-RVRLEEQERQ-QQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEE 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 431 NKQQLDELKDYMKYLTKRCDVDVAELSEALLLIKVRKEQKKNGDLICLEKDDDDIQKVSERSMRklqlahaetVQELEKT 510
Cdd:pfam17380 504 RKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSR---------LEAMERE 574
|
330 340 350
....*....|....*....|....*....|....*....
gi 2024349574 511 RSMLiVQHKINKGYQTEIEAVTQkMESLQKDYELKIGKY 549
Cdd:pfam17380 575 REMM-RQIVESEKARAEYEATTP-ITTIKPIYRPRISEY 611
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
269-564 |
6.54e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.84 E-value: 6.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 269 RKQLAEKSSALAAMESKFLQLQENQRNFKTNHDVLIAKSEELNVQLKEERSKCLHLEKELQSVaisKRRTEELEERVNDL 348
Cdd:TIGR02169 673 PAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKL---KERLEELEEDLSSL 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 349 EREKELLKENCDKLSSsvfsmtREQEWKLKEEQLKLQIAELETAI-QSSLADKDEILGKLKVERDKKEKLMEE-NKDLQS 426
Cdd:TIGR02169 750 EQEIENVKSELKELEA------RIEELEEDLHKLEEALNDLEARLsHSRIPEIQAELSKLEEEVSRIEARLREiEQKLNR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 427 CYLEnKQQLDELKDYMKYLTKRCDVDVAELSEALLLIKVRKEQKK-------------NGDLICLEKDDDDIQKVSERSM 493
Cdd:TIGR02169 824 LTLE-KEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEeeleeleaalrdlESRLGDLKKERDELEAQLRELE 902
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024349574 494 RKLQLAHAEtVQELEKTRSMLIVQHKINKGYQTEIEAVTQKMESLQKDyELKIGKYVDLLDMKAARIKKLE 564
Cdd:TIGR02169 903 RKIEELEAQ-IEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEE-ELSLEDVQAELQRVEEEIRALE 971
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
305-567 |
7.32e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.44 E-value: 7.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 305 AKSEELNVQLKEERSKCLHLEKELQSVaisKRRTEELEERVNDLEREKELLKENCDKLSSSVFSMTREQE-WKLKEEQLK 383
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAEL---RKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEqLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 384 LQIAELETAIQSSLADKDEILGKLKVERDKKEKLMEENKDLQSCYLENKQQLDELKDymkyltkrcdvDVAELSEALLLI 463
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA-----------ELTLLNEEAANL 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 464 KVRKEQKKNgDLICLEKDDDDIQKVSER---SMRKLQLAHAETVQELEKTRSMLIVQHKINKGYQTEIEAVTQKMESLQ- 539
Cdd:TIGR02168 823 RERLESLER-RIAATERRLEDLEEQIEElseDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSe 901
|
250 260 270
....*....|....*....|....*....|
gi 2024349574 540 --KDYELKIGKYVDLLDMKAARIKKLEAQL 567
Cdd:TIGR02168 902 elRELESKRSELRRELEELREKLAQLELRL 931
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
198-570 |
1.41e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 49.63 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 198 LEDARAKIRNLETVIDSQRGRIQEL-----EHLSELLGSQLRNKEKEIEESALHLKEQEAA-----RQRSNIRD-----N 262
Cdd:TIGR04523 276 LEQNNKKIKELEKQLNQLKSEISDLnnqkeQDWNKELKSELKNQEKKLEEIQNQISQNNKIisqlnEQISQLKKeltnsE 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 263 VEMIKVRKQLAEKSSALAAMESkflqlqENQRNFKTNHDvLIAKSEELNVQLKEErskclhlekelqsvaisKRRTEELE 342
Cdd:TIGR04523 356 SENSEKQRELEEKQNEIEKLKK------ENQSYKQEIKN-LESQINDLESKIQNQ-----------------EKLNQQKD 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 343 ERVNDLEREKELLKENCDKLsssvfsmtREQEWKLKEE--QLKLQIAELETAIQSSLADKDEILGKLKVERDKKEKLMEE 420
Cdd:TIGR04523 412 EQIKKLQQEKELLEKEIERL--------KETIIKNNSEikDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQN 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 421 NKDLQSCYLENKQQLDELKDYMKYLTKRCDVDVAELSEALLLIKVRKEQKKNGDLICLEKDDDDIQKVSERSMRKLQlah 500
Cdd:TIGR04523 484 LEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLE--- 560
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 501 aETVQELEKTrsmlIVQHKINkgyQTEIEAVTQKMESLQKDYELKIGKYVDLLDMKAARIKKLEAQLRDV 570
Cdd:TIGR04523 561 -KEIDEKNKE----IEELKQT---QKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKA 622
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
45-379 |
2.25e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.90 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 45 RKELEDKYLQLRDENISLKQHANKQEETIKRMATRLIQLVH-DKKRNEQVGGGPKRLGRTVKMEGMVEHLQERVRDLEKQ 123
Cdd:TIGR02168 718 RKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTElEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEE 797
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 124 NEILRSKLISNKQQIHMPSHRPIQYKFAQPRNSNGLKKASDAAGTPEPTKKGMRLQNLEVRSpplvlrrcgpnLLEDARA 203
Cdd:TIGR02168 798 LKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA-----------EIEELEE 866
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 204 KIRNLETVIDSQRGRIQELEHLSELLGSQLRNKEKEIEESALHLKEQEAARQRSnirdnvemikvRKQLAEKSSALAAME 283
Cdd:TIGR02168 867 LIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEEL-----------REKLAQLELRLEGLE 935
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 284 SKFLQLQENQRN-FKTNHDVLIAKSEELNVQLKEERSKCLHLEKELQSV------AISKrrTEELEERVNDLEREKELLK 356
Cdd:TIGR02168 936 VRIDNLQERLSEeYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELgpvnlaAIEE--YEELKERYDFLTAQKEDLT 1013
|
330 340
....*....|....*....|...
gi 2024349574 357 ENCDKLSSSVFSMTREQEWKLKE 379
Cdd:TIGR02168 1014 EAKETLEEAIEEIDREARERFKD 1036
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
203-570 |
2.33e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 49.02 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 203 AKIRNLETVIDSQRGRIQELEHLSELLGSQLRNKEKEIEESALHLKEQEAARQRSNIRDNVEMIKVRKqlaekssalaaM 282
Cdd:pfam01576 68 ARKQELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKK-----------L 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 283 ESKFLQLQENQRNFKTNHDVLIAKSEELNVQL--KEERSKCLHLEKELQSVAISkrrteELEERVNDLEREKELLKENCD 360
Cdd:pfam01576 137 EEDILLLEDQNSKLSKERKLLEERISEFTSNLaeEEEKAKSLSKLKNKHEAMIS-----DLEERLKKEEKGRQELEKAKR 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 361 KLSSSvFSMTREQ--EWKLKEEQLKLQIAELETAIQSSLADKDEilgklkvERDKKEKLMEENKDLQSCYLENKQQLDEL 438
Cdd:pfam01576 212 KLEGE-STDLQEQiaELQAQIAELRAQLAKKEEELQAALARLEE-------ETAQKNNALKKIRELEAQISELQEDLESE 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 439 KDYMKYLTKRCDvDVAELSEAL------LLIKVRKEQ----KKNGDLICLEKDDDDIQKVSERSMRKLQLAHAETVQEL- 507
Cdd:pfam01576 284 RAARNKAEKQRR-DLGEELEALkteledTLDTTAAQQelrsKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELt 362
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024349574 508 -------------EKTRSMLivqHKINKGYQTEIEAVTQ-KMESLQKDyelkigkyvdlldmkaariKKLEAQLRDV 570
Cdd:pfam01576 363 eqleqakrnkanlEKAKQAL---ESENAELQAELRTLQQaKQDSEHKR-------------------KKLEGQLQEL 417
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
314-569 |
2.96e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 48.39 E-value: 2.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 314 LKEERSKC---LHlekELQSVAISKRRTEELEERVNDLEREKELLKENCDKLSSSVfsmtrEQEWKLKEEQLKLQIAELE 390
Cdd:PRK05771 14 LKSYKDEVleaLH---ELGVVHIEDLKEELSNERLRKLRSLLTKLSEALDKLRSYL-----PKLNPLREEKKKVSVKSLE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 391 TAIQSSLADKDEILGKLKVERDKKEKLMEENKDLQScyleNKQQLDELKDY---MKYLTKRCDVDV------AELSEALL 461
Cdd:PRK05771 86 ELIKDVEEELEKIEKEIKELEEEISELENEIKELEQ----EIERLEPWGNFdldLSLLLGFKYVSVfvgtvpEDKLEELK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 462 LIKVRK-----EQKKNGD---LICLEKDDDDIQKVSER-SMRKLQLAHAETVQE-LEKTRSMLIvqhKINKgyqtEIEAV 531
Cdd:PRK05771 162 LESDVEnveyiSTDKGYVyvvVVVLKELSDEVEEELKKlGFERLELEEEGTPSElIREIKEELE---EIEK----ERESL 234
|
250 260 270
....*....|....*....|....*....|....*...
gi 2024349574 532 TQKMESLQKDYELKIGKYVDLLDMKAARIKKLEAQLRD 569
Cdd:PRK05771 235 LEELKELAKKYLEELLALYEYLEIELERAEALSKFLKT 272
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
196-568 |
3.19e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.48 E-value: 3.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 196 NLLEDARAKIRNLETVIDSQRGRIQELEHLSELLGSQLRNKEKEIeesalHLKEQEAARQRSNIRDNVEMI-KVRKQLAE 274
Cdd:TIGR04523 75 NKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQK-----NKLEVELNKLEKQKKENKKNIdKFLTEIKK 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 275 KSSALAAMESKFLQLQENQRNFKTNHDVLIAKSEELNVQLKEERSKCLHLEKELQSVAISKRRTEELEERVNDLEREKEL 354
Cdd:TIGR04523 150 KEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQ 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 355 LKENCDKLSS------SVFSMTREQEWKLKEE------QLKLQIAELETAiQSSLADKDEILGKLKVERD--KKEKLMEE 420
Cdd:TIGR04523 230 LKDNIEKKQQeinektTEISNTQTQLNQLKDEqnkikkQLSEKQKELEQN-NKKIKELEKQLNQLKSEISdlNNQKEQDW 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 421 NKDLQSCYLENKQQLDELKDymkyltkrcdvdvaELSEALLLIKVRKEQKKNgdlicLEKDDDDiqKVSERSMRKLQLah 500
Cdd:TIGR04523 309 NKELKSELKNQEKKLEEIQN--------------QISQNNKIISQLNEQISQ-----LKKELTN--SESENSEKQREL-- 365
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024349574 501 AETVQELEKTRsmlivqhKINKGYQTEIeavtQKMESLQKDYELKIGKYVDLLDMKAARIKKLEAQLR 568
Cdd:TIGR04523 366 EEKQNEIEKLK-------KENQSYKQEI----KNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKE 422
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
337-540 |
3.19e-05 |
|
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: 47.97 E-value: 3.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 337 RTEELEERVNDLEREKELLKENCDKLSSSvfSMTREQEWKLKEEQLKLQIAELETAIQSSLADKDEILGKLKVERDKKEK 416
Cdd:pfam07888 35 RLEECLQERAELLQAQEAANRQREKEKER--YKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 417 LMEENKDLQSCYLENKQQLDELKDYMKYLTKRCDVDVAELSeallliKVRKEQKKngdLICLEKDDDDIQKVSERSMRKL 496
Cdd:pfam07888 113 LSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELE------RMKERAKK---AGAQRKEEEAERKQLQAKLQQT 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2024349574 497 QLAHAETVQELEKTRSMLIVQHKINKGYQTEIEAVTQKMESLQK 540
Cdd:pfam07888 184 EEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHR 227
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
195-366 |
3.77e-05 |
|
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: 46.46 E-value: 3.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 195 PNLLEDARAKIRNLETVIDSQRGRIQELEhlsellgSQLRNKEKEIEESALHLKEQEAarQRSNIRDNVEMIKVRKQLAE 274
Cdd:COG1579 30 PAELAELEDELAALEARLEAAKTELEDLE-------KEIKRLELEIEEVEARIKKYEE--QLGNVRNNKEYEALQKEIES 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 275 KSSALAAMESKFLQLQEnqrnfktnhdvliaKSEELNVQLKEERSKCLHLEKELqsvaisKRRTEELEERVNDLEREKEL 354
Cdd:COG1579 101 LKRRISDLEDEILELME--------------RIEELEEELAELEAELAELEAEL------EEKKAELDEELAELEAELEE 160
|
170
....*....|..
gi 2024349574 355 LKENCDKLSSSV 366
Cdd:COG1579 161 LEAEREELAAKI 172
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
46-353 |
3.90e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.13 E-value: 3.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 46 KELEDKYLQLRDENISLKQHANKQEETIKRMATRLIQLVHDKKRNEQVGGGPK----RLGRTV-KMEGMVEHLQERVRDL 120
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRkdlaRLEAEVeQLEERIAQLSKELTEL 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 121 EKQNEILRSKLISNKQQIHmPSHRPIQYKFAQPRNSNGLKKASDAAGTpeptKKGMRLQNLEVRSPPLVLRRCG-PNLLE 199
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELA-EAEAEIEELEAQIEQLKEELKALREALD----ELRAELTLLNEEAANLRERLESlERRIA 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 200 DARAKIRNLETVIDSQRGRIQELEHLSELLGSQLRNKEKEIEEsalHLKEQEAARQRsnirdnveMIKVRKQLAEKSSAL 279
Cdd:TIGR02168 835 ATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEA---LLNERASLEEA--------LALLRSELEELSEEL 903
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024349574 280 AAMESKFLQLQENQRNFKTNHDVLIAKSEELNVQLKEERSKC-----LHLEKELQSVAISKRRTEELEERVNDLEREKE 353
Cdd:TIGR02168 904 RELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLseeysLTLEEAEALENKIEDDEEEARRRLKRLENKIK 982
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
176-414 |
4.30e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 47.97 E-value: 4.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 176 MRLQNLEVRSPPLVLRRCGPNLLEDARAKIRNlETVIDSQRGRIQELEHLSELlgSQLRNKEKEIEESALHLKEQeaarq 255
Cdd:PLN02939 177 MRLSETDARIKLAAQEKIHVEILEEQLEKLRN-ELLIRGATEGLCVHSLSKEL--DVLKEENMLLKDDIQFLKAE----- 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 256 RSNIRDNVE-MIKVRKQLAEKSSALAAMESKFLQLQENQRNFKT-NHDVLIAKSEELNVQLKEerskclhLEKELQSVAI 333
Cdd:PLN02939 249 LIEVAETEErVFKLEKERSLLDASLRELESKFIVAQEDVSKLSPlQYDCWWEKVENLQDLLDR-------ATNQVEKAAL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 334 SKRRTEELEERVNDLErekELLKE-NCDKLSSSVFSMTrEQEWKLKEEQLKLQIAELETAI---QSSLADKDEILGKLKV 409
Cdd:PLN02939 322 VLDQNQDLRDKVDKLE---ASLKEaNVSKFSSYKVELL-QQKLKLLEERLQASDHEIHSYIqlyQESIKEFQDTLSKLKE 397
|
....*
gi 2024349574 410 ERDKK 414
Cdd:PLN02939 398 ESKKR 402
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
132-456 |
4.97e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 47.97 E-value: 4.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 132 ISNKQQIHMPSHR--PIQYKFAQPRNSNGLKKASDAAGTPE--PTKKGMRLQNLEVRSPPLVLRRCGPNLLEDAR--AKI 205
Cdd:PLN02939 17 IRSRAPFYLPSRRrlAVSCRARRRGFSSQQKKKRGKNIAPKqrSSNSKLQSNTDENGQLENTSLRTVMELPQKSTssDDD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 206 RNLETVI---------DSQRGRIQELEHLSEL----LGSQLRNKEKEI-----------EESALHLKEQEAARQRSNIrd 261
Cdd:PLN02939 97 HNRASMQrdeaiaaidNEQQTNSKDGEQLSDFqledLVGMIQNAEKNIlllnqarlqalEDLEKILTEKEALQGKINI-- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 262 nVEMikvRKQLAEKSSALAAMESKFLQLQENQRNFKTNH---------DVLIAKSEELNVqLKEE----RSKCLHLEKEL 328
Cdd:PLN02939 175 -LEM---RLSETDARIKLAAQEKIHVEILEEQLEKLRNEllirgategLCVHSLSKELDV-LKEEnmllKDDIQFLKAEL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 329 QSVAiskrrteELEERVNDLEREKELLKENCDKLSSSvFSMTREQEWKLKEEQLKLQIAELET--AIQSSLADKDE---- 402
Cdd:PLN02939 250 IEVA-------ETEERVFKLEKERSLLDASLRELESK-FIVAQEDVSKLSPLQYDCWWEKVENlqDLLDRATNQVEkaal 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2024349574 403 ILGKLKVERDKKEKLmEENKDLQSCYLENKQQLDELKDYMKYLTKRCDVDVAEL 456
Cdd:PLN02939 322 VLDQNQDLRDKVDKL-EASLKEANVSKFSSYKVELLQQKLKLLEERLQASDHEI 374
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
20-415 |
9.10e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 47.04 E-value: 9.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 20 TLPRVRGLLASARNVKA--RQAVSQFSRKE--LEDKYLQLRDENISLKQHANKQEET---IKRMATR----LIQLVHDKK 88
Cdd:pfam15921 459 SLEKVSSLTAQLESTKEmlRKVVEELTAKKmtLESSERTVSDLTASLQEKERAIEATnaeITKLRSRvdlkLQELQHLKN 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 89 RNEQVgggpkrlgRTVKMEgmVEHLQERVRDLEKQNEILRSKlISNKQQI---HMPSHRPIQYKFAQPRNSNGLKKASDA 165
Cdd:pfam15921 539 EGDHL--------RNVQTE--CEALKLQMAEKDKVIEILRQQ-IENMTQLvgqHGRTAGAMQVEKAQLEKEINDRRLELQ 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 166 AGTPEPTKKGMRLQNLEVRSPPLVLRR-----CGPNLL---EDARAKIRNLETVIDSQRGRIQELEHLSELLGSQLRNKE 237
Cdd:pfam15921 608 EFKILKDKKDAKIRELEARVSDLELEKvklvnAGSERLravKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKS 687
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 238 KEIEESALHLKEQEAARQrsnirdnvemikvrKQLAEKSSALAAMESKflqlqenqrnfkTNHDVLIAKSeeLNVQLKEE 317
Cdd:pfam15921 688 EEMETTTNKLKMQLKSAQ--------------SELEQTRNTLKSMEGS------------DGHAMKVAMG--MQKQITAK 739
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 318 RSKCLHLEKELQSvaiskrrteeLEERVNDLEREKELLKENCDKLSSSV-------------FSMTREQEWKLKE----- 379
Cdd:pfam15921 740 RGQIDALQSKIQF----------LEEAMTNANKEKHFLKEEKNKLSQELstvateknkmageLEVLRSQERRLKEkvanm 809
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2024349574 380 ----EQLKLQIAELETAIQSSlaDKDEILGKLKVERDKKE 415
Cdd:pfam15921 810 evalDKASLQFAECQDIIQRQ--EQESVRLKLQHTLDVKE 847
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
199-362 |
9.65e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.30 E-value: 9.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 199 EDARAKIRNLETVIDSQRGRIQELEHLSELLGSQLRNKEKEIEESALHLKEQEA-------ARQRSNIRDNVEMIKVRKQ 271
Cdd:COG4942 51 KALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEelaellrALYRLGRQPPLALLLSPED 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 272 LAEKSSALA-------AMESKFLQLQENQRNFKTNHDVLIAKSEELNVQLKEERSKCLHLEKELQS----VAISKRRTEE 340
Cdd:COG4942 131 FLDAVRRLQylkylapARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAErqklLARLEKELAE 210
|
170 180
....*....|....*....|..
gi 2024349574 341 LEERVNDLEREKELLKENCDKL 362
Cdd:COG4942 211 LAAELAELQQEAEELEALIARL 232
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
42-432 |
1.01e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 46.64 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 42 QFSRKELEDKYLQLRDENISlKQHANKQEETIKrmatrlIQLVHDKKRNEQVGGGPKRLgrTVKMEGMVEHLQERVRDLE 121
Cdd:pfam05483 446 QAREKEIHDLEIQLTAIKTS-EEHYLKEVEDLK------TELEKEKLKNIELTAHCDKL--LLENKELTQEASDMTLELK 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 122 KQNEilrsKLISNKQQIH--MPSHRPIQYKFAQPRNSnglkkasdaagtPEPTKKGMRLQNLEVRSPplvlrrcgpnlLE 199
Cdd:pfam05483 517 KHQE----DIINCKKQEErmLKQIENLEEKEMNLRDE------------LESVREEFIQKGDEVKCK-----------LD 569
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 200 DARAKIRNLETVIDSQRGRIQELEHLSELLGSQLRNKEKEIEEsaLHlKEQEAARQRSNIRD---NVEMIKVRKQLAEKS 276
Cdd:pfam05483 570 KSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEE--LH-QENKALKKKGSAENkqlNAYEIKVNKLELELA 646
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 277 SALAAMESKFLQLQENQRNFKTNHDVLIAKSEELNVQLKEerskCLHLEKElqsvaISKRRTEELEERVNDLEREKELLK 356
Cdd:pfam05483 647 SAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADE----AVKLQKE-----IDKRCQHKIAEMVALMEKHKHQYD 717
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024349574 357 ENCDKLSSSV-FSMTREQEWKLKEEQLKLQIAELETAIQSsladkdeILGKLKVERDKKEKLMEENKDLQSCYLENK 432
Cdd:pfam05483 718 KIIEERDSELgLYKNKEQEQSSAKAALEIELSNIKAELLS-------LKKQLEIEKEEKEKLKMEAKENTAILKDKK 787
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
198-571 |
1.24e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 198 LEDARAKIRNLEtvidSQRGRIQELEHLSELLGSQLRNKEKEIEESALHLKEQEAARQrsnirdNVEMIKVRKQLAEKss 277
Cdd:COG4717 73 LKELEEELKEAE----EKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ------LLPLYQELEALEAE-- 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 278 aLAAMESKFLQLQENQRNFKTnhdvLIAKSEELNVQLKEERSKCLHLEKEL-----QSVAISKRRTEELEERVNDLEREK 352
Cdd:COG4717 141 -LAELPERLEELEERLEELRE----LEEELEELEAELAELQEELEELLEQLslateEELQDLAEELEELQQRLAELEEEL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 353 ELLKENCDKLSSSVFSMTREQEWKLKEEQLKLQ---------IAELETAIQSSLADKDEILGKLKV-----------ERD 412
Cdd:COG4717 216 EEAQEELEELEEELEQLENELEAAALEERLKEArlllliaaaLLALLGLGGSLLSLILTIAGVLFLvlgllallfllLAR 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 413 KKEKLMEENKDLQSCYLENKQQLDELKDYMKYLTKRCDVDVAELSEALLLIKVRKEQKKNgdlicLEKDDDDIQKVSERS 492
Cdd:COG4717 296 EKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLRE-----AEELEEELQLEELEQ 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 493 MRK--LQLAHAETVQELEKtrsmLIVQHKINKGYQTEIEAVTQKMESLQKDYElKIGKYVDLLDMKaARIKKLEAQLRDV 570
Cdd:COG4717 371 EIAalLAEAGVEDEEELRA----ALEQAEEYQELKEELEELEEQLEELLGELE-ELLEALDEEELE-EELEELEEELEEL 444
|
.
gi 2024349574 571 A 571
Cdd:COG4717 445 E 445
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
229-623 |
2.04e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.28 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 229 LGSQLRNKEKEIEESALHLKEQEAARQRSNIRDNVEMIKVRKQLAEKSSALAAMESKFLQLQENQRNFKTNHDVLIAKSE 308
Cdd:COG4372 4 LGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 309 ELNVQLKEERSKCLHLEKELQSVaisKRRTEELEERVNDLEREKELLKEncdklsssvfsmtreqewklKEEQLKLQIAE 388
Cdd:COG4372 84 ELNEQLQAAQAELAQAQEELESL---QEEAEELQEELEELQKERQDLEQ--------------------QRKQLEAQIAE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 389 LETAIQSSLADKDEILGKLKVERDKKEKLMEENKdlqscYLENKQQLDELKDYMKYLTKRCDVDVAELSEALLLIKVRKE 468
Cdd:COG4372 141 LQSEIAEREEELKELEEQLESLQEELAALEQELQ-----ALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 469 QKKNGDLICLEKDDDDIQKVSERSMRKLQLAHAETVQELEKTRSMLIVQHKINKGYQTEIEAVTQKMESLQKDYELKIGK 548
Cdd:COG4372 216 LAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALEL 295
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024349574 549 YVDLLDMKAARIKKLEAQLRDVAYGSKRYKFRPEILPANPVNIFDETLHFERREGLFEIHISKVIFSSEAVHAFG 623
Cdd:COG4372 296 KLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
220-576 |
2.10e-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: 45.73 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 220 QELEHLSELLGSQLRNKEKEIEESALHLKEQEAARQRSNIRDNVEMIKVRKQLAEksSALAAMESKFLQLQENQRNFKTN 299
Cdd:TIGR00618 591 NITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKL--TALHALQLTLTQERVREHALSIR 668
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 300 HDVLIAKSEELNvQLKEERSKCLHLEKELQSVAISKRRTEELEERVNDLERE-----------KELLKENCDKLSSSVFS 368
Cdd:TIGR00618 669 VLPKELLASRQL-ALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREfneienassslGSDLAAREDALNQSLKE 747
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 369 MTREQEWKLKEEQLKLQIAELETAIQSSLADKdeiLGKLKVERDKKEKLMEEnkDLQSCYLENKQQLDELKDYMKYLTKR 448
Cdd:TIGR00618 748 LMHQARTVLKARTEAHFNNNEEVTAALQTGAE---LSHLAAEIQFFNRLREE--DTHLLKTLEAEIGQEIPSDEDILNLQ 822
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 449 CDVDVAELSEalLLIKVRKEQKKNGDLICLEKDDDDIQKVSERSMRKlqlaHAETVQELEKT--RSMLIVQHKINKGYQT 526
Cdd:TIGR00618 823 CETLVQEEEQ--FLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQE----QAKIIQLSDKLngINQIKIQFDGDALIKF 896
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 2024349574 527 EIEAVTQKMESLQKDYELKI-GKYvdLLDMKAARIKKLEAQLRDVAYGSKR 576
Cdd:TIGR00618 897 LHEITLYANVRLANQSEGRFhGRY--ADSHVNARKYQGLALLVADAYTGSV 945
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
199-514 |
2.39e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 199 EDARAKIRNLETVIDSQRGRIQELEHLSELLgSQLRNK----EKEIEESALHLKEQEAAR-----QRSNIRDNVEMIK-- 267
Cdd:PRK02224 230 EQARETRDEADEVLEEHEERREELETLEAEI-EDLRETiaetEREREELAEEVRDLRERLeeleeERDDLLAEAGLDDad 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 268 ---VRKQLAEKSSALAAMESKFLQLQENQRNFKTNHDVLIAKSEELNVQLKEERSKCLHLEKELQS--VAISKRRT---- 338
Cdd:PRK02224 309 aeaVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEarEAVEDRREeiee 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 339 -----EELEERVND-------LEREKELLKENCDKLSSSVfsmtREQEWKLKEEQLKLQIAEL---------------ET 391
Cdd:PRK02224 389 leeeiEELRERFGDapvdlgnAEDFLEELREERDELRERE----AELEATLRTARERVEEAEAlleagkcpecgqpveGS 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 392 AIQSSLADKDEILGKL-------KVERDKKEKLMEENKDLQscylENKQQLDELKDYMKYLTKRCDVDVAELSEALLLIK 464
Cdd:PRK02224 465 PHVETIEEDRERVEELeaeledlEEEVEEVEERLERAEDLV----EAEDRIERLEERREDLEELIAERRETIEEKRERAE 540
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2024349574 465 VRKEQKKNgdlicLEKDDDDIQKVSERSMRKLQlAHAETVQELEKTRSML 514
Cdd:PRK02224 541 ELRERAAE-----LEAEAEEKREAAAEAEEEAE-EAREEVAELNSKLAEL 584
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
46-363 |
6.81e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.28 E-value: 6.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 46 KELEDKYLQLRDENISLKQHANKQEETIKRMATRLIQLVHDK-KRNEQVGGGPKRLGRTV----KMEGMVEHLQERVRDL 120
Cdd:TIGR02168 235 EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVsELEEEIEELQKELYALAneisRLEQQKQILRERLANL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 121 EKQNEILRSKLISNKQQihmpshrPIQYKFAqprnsngLKKASDAAGTPEPTKKGMRlqnlevrspplvlrrcgpNLLED 200
Cdd:TIGR02168 315 ERQLEELEAQLEELESK-------LDELAEE-------LAELEEKLEELKEELESLE------------------AELEE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 201 ARAKIRNLET-------VIDSQRGRIQELEHLSELLGSQLRNKEKEIEESalhlkEQEAARQRSNIRDNvEMIKVRKQLA 273
Cdd:TIGR02168 363 LEAELEELESrleeleeQLETLRSKVAQLELQIASLNNEIERLEARLERL-----EDRRERLQQEIEEL-LKKLEEAELK 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 274 EKSSALAAMESKFLQLQEnqrnfktNHDVLIAKSEELNVQLKEERSKCLHLEKELQSVAISKRRTEELEERVNDLEREKE 353
Cdd:TIGR02168 437 ELQAELEELEEELEELQE-------ELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVK 509
|
330
....*....|
gi 2024349574 354 LLKENCDKLS 363
Cdd:TIGR02168 510 ALLKNQSGLS 519
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
233-497 |
7.77e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.98 E-value: 7.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 233 LRNKEKEIEESALHLKEQ-----EAARQRSNIRDnvemiKVRKQLAEKSSALAAMESKFLQLQENQRNFKTNHDVLIAKS 307
Cdd:COG1340 13 LEEKIEELREEIEELKEKrdelnEELKELAEKRD-----ELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 308 EELNVQLKEERSKCLHLEKELQSVAISKRRTEELEER----VNDLEREKEL------LKENCDKLSSSvfsmtREQEWKL 377
Cdd:COG1340 88 NELREELDELRKELAELNKAGGSIDKLRKEIERLEWRqqteVLSPEEEKELvekikeLEKELEKAKKA-----LEKNEKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 378 KE-----EQLKLQIAELETAIQSSLADKDEILGKLKVERDKKEKLMEENKDLQSCYLENKQQLDELKdymkyltKRCDVD 452
Cdd:COG1340 163 KElraelKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELH-------EEIIEL 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2024349574 453 VAELSEallLIKVRKEQKKNGDLICLEKDDDDIQKVSERSMRKLQ 497
Cdd:COG1340 236 QKELRE---LRKELKKLRKKQRALKREKEKEELEEKAEEIFEKLK 277
|
|
| C2A_Ferlin |
cd08373 |
C2 domain first repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and ... |
819-921 |
8.79e-04 |
|
C2 domain first repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and other proteins, such as Synaptotagmins, are implicated in facilitating the fusion process when cell membranes fuse together. There are six known human Ferlins: Dysferlin (Fer1L1), Otoferlin (Fer1L2), Myoferlin (Fer1L3), Fer1L4, Fer1L5, and Fer1L6. Defects in these genes can lead to a wide range of diseases including muscular dystrophy (dysferlin), deafness (otoferlin), and infertility (fer-1, fertilization factor-1). Structurally they have 6 tandem C2 domains, designated as (C2A-C2F) and a single C-terminal transmembrane domain, though there is a new study that disputes this and claims that there are actually 7 tandem C2 domains with another C2 domain inserted between C2D and C2E. In a subset of them (Dysferlin, Myoferlin, and Fer1) there is an additional conserved domain called DysF. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-II topology.
Pssm-ID: 176019 [Multi-domain] Cd Length: 127 Bit Score: 40.70 E-value: 8.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 819 HDTRIIPSSSNPQIDDHmcFQVPMTADLDQYlkwESLTFYVFDDSEMGEDGFLGKANVPLIPLACNRSISGTFEVTDSER 898
Cdd:cd08373 28 KKTRVLENELNPVWNET--FEWPLAGSPDPD---ESLEIVVKDYEKVGRNRLIGSATVSLQDLVSEGLLEVTEPLLDSNG 102
|
90 100
....*....|....*....|....
gi 2024349574 899 RVTGA-IRVELKwkfaYLSPSGAA 921
Cdd:cd08373 103 RPTGAtISLEVS----YQPPDGAV 122
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
218-420 |
8.84e-04 |
|
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: 43.35 E-value: 8.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 218 RIQELEHLSELLGSQLRNKEKEIE-------ESALHLKEQEAARQRSNIR---DNVEMIKVRKQLAEKSSALAAMESKFL 287
Cdd:pfam07888 130 RIRELEEDIKTLTQRVLERETELErmkerakKAGAQRKEEEAERKQLQAKlqqTEEELRSLSKEFQELRNSLAQRDTQVL 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 288 QLQENQRNFKTNHDVLIAKSEELNVQLKEERSkclhlekelqsvaiskrrteeLEERVNDLEREKELLKENcdkLSSSVF 367
Cdd:pfam07888 210 QLQDTITTLTQKLTTAHRKEAENEALLEELRS---------------------LQERLNASERKVEGLGEE---LSSMAA 265
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024349574 368 SMTREQ----EWKLKEEQLKLQIAEL---------------ETAIQSSLADKDEILgKLKVERDKKEKLMEE 420
Cdd:pfam07888 266 QRDRTQaelhQARLQAAQLTLQLADAslalregrarwaqerETLQQSAEADKDRIE-KLSAELQRLEERLQE 336
|
|
| C2_C21orf25-like |
cd08678 |
C2 domain found in the Human chromosome 21 open reading frame 25 (C21orf25) protein; The ... |
819-918 |
1.00e-03 |
|
C2 domain found in the Human chromosome 21 open reading frame 25 (C21orf25) protein; The members in this cd are named after the Human C21orf25 which contains a single C2 domain. Several other members contain a C1 domain downstream of the C2 domain. No other information on this protein is currently known. The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.
Pssm-ID: 176060 [Multi-domain] Cd Length: 126 Bit Score: 40.43 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 819 HDTRIIPSSSNPQIDDHMCFQV-PMTADLdqylkweslTFYVFDDSEMGEDGFLGKANVPLIPLACNRSISGTFE---VT 894
Cdd:cd08678 33 YQSSTQKNTSNPFWDEHFLFELsPNSKEL---------LFEVYDNGKKSDSKFLGLAIVPFDELRKNPSGRQIFPlqgRP 103
|
90 100
....*....|....*....|....
gi 2024349574 895 DSERRVTGAIRVElkwkFAYLSPS 918
Cdd:cd08678 104 YEGDSVSGSITVE----FLFMEPA 123
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
200-584 |
1.30e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 43.29 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 200 DARAKIRNLETVIDSQRGRiqELEHLSELLGSQLRNKEKEIEESALHLKEQEAArqrsnIRDNVEMIKVRKQLAEKSSAL 279
Cdd:pfam12128 372 DVTAKYNRRRSKIKEQNNR--DIAGIKDKLAKIREARDRQLAVAEDDLQALESE-----LREQLEAGKLEFNEEEYRLKS 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 280 AAMESKFLQ--------LQENQRNF------------KTNHDVLIAKSEELnvQLKEERSKCL-HLEKELQSVAISKRRT 338
Cdd:pfam12128 445 RLGELKLRLnqatatpeLLLQLENFderierareeqeAANAEVERLQSELR--QARKRRDQASeALRQASRRLEERQSAL 522
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 339 EELEERVND--------LEREKELLKENCDKLSSS----------------------VFSMTRE------QEWKLKEEQL 382
Cdd:pfam12128 523 DELELQLFPqagtllhfLRKEAPDWEQSIGKVISPellhrtdldpevwdgsvggelnLYGVKLDlkridvPEWAASEEEL 602
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 383 KLQIAELETAIQS---SLADKDEILGKLKVERDKKEKLMEenkDLQSCYLENKQQLDELKDYMKYLTKRCDVDVAELSEA 459
Cdd:pfam12128 603 RERLDKAEEALQSareKQAAAEEQLVQANGELEKASREET---FARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDS 679
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 460 llliKVRKEQKKNGDLICLEKDDDDIQKVSERSMRKLQLAHAETVQELEKTRSMLIVQhkINKGYQTEIEAVTQKMESLQ 539
Cdd:pfam12128 680 ----ANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLAL--LKAAIAARRSGAKAELKALE 753
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 2024349574 540 KDY--ELKiGKYVD---LLDMKaARIKKLEAQLRDVAygskryKFRPEIL 584
Cdd:pfam12128 754 TWYkrDLA-SLGVDpdvIAKLK-REIRTLERKIERIA------VRRQEVL 795
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
264-420 |
1.38e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.83 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 264 EMIKVRKQLAEKSSALAAMESKFLQLQENQRNFKTNHDVLIAKSEELNVQLKEERSKCLHLEKELQSVaiskRRTEELEe 343
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV----RNNKEYE- 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024349574 344 rvnDLEREKELLKENCDKLSSSVFS-MTREQEWKLKEEQLKLQIAELETAIQSSLADKDEILGKLKVERDKKEKLMEE 420
Cdd:COG1579 93 ---ALQKEIESLKRRISDLEDEILElMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREE 167
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
309-461 |
1.41e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.83 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 309 ELNVQLKEERSKCLHLEKELQSVaisKRRTEELEERVNDLEREKELLKENCDKLS----------SSVFSmTREQEWKLK 378
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAAL---EARLEAAKTELEDLEKEIKRLELEIEEVEarikkyeeqlGNVRN-NKEYEALQK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 379 E-EQLKLQIAELETAIQSSLADKDEILGKLKVERDKKEKLMEENKDLQScylENKQQLDELKDYMKYLTKRCDVDVAELS 457
Cdd:COG1579 97 EiESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKA---ELDEELAELEAELEELEAEREELAAKIP 173
|
....
gi 2024349574 458 EALL 461
Cdd:COG1579 174 PELL 177
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
211-472 |
2.43e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.31 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 211 VIDSQRGRIQELEHLSELLGSQLRNKEKEIEESALHLKEQEAARQRSNirdnvEMIKVRKQlaekssalaamESKFLQLQ 290
Cdd:TIGR04523 27 IANKQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSN-----NKIKILEQ-----------QIKDLNDK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 291 ENQRNFKTNHdvLIAKSEELNVQLKEERSKCLHLEKELQSVAISKRRTEELEERVND-LEREKELLKEncdklSSSVFSM 369
Cdd:TIGR04523 91 LKKNKDKINK--LNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTeIKKKEKELEK-----LNNKYND 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 370 TREQEWKLKEEQLKLqiaeletaiQSSLADKDEILGKLKVERDKKEKLM-------EENKDLQSCYLENKQQLDELKDYM 442
Cdd:TIGR04523 164 LKKQKEELENELNLL---------EKEKLNIQKNIDKIKNKLLKLELLLsnlkkkiQKNKSLESQISELKKQNNQLKDNI 234
|
250 260 270
....*....|....*....|....*....|
gi 2024349574 443 KYLTKRCDVDVAELSEALLLIKVRKEQKKN 472
Cdd:TIGR04523 235 EKKQQEINEKTTEISNTQTQLNQLKDEQNK 264
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
380-569 |
2.52e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.67 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 380 EQLKLQIAELETAIQSSLADKDEILGKLKVERDKKEKLMEENKDLQSCYLENKQQLDELKDYMKYLTKRCDVDVAELSEa 459
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 460 lLLIKVRKEQKKNGDLICLEKDDDDIQKVSERSMRKLQLAHAETVQELEKTRSMLIVQHKINKGYQTEIEAVTQKMESLQ 539
Cdd:COG4942 109 -LLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEER 187
|
170 180 190
....*....|....*....|....*....|
gi 2024349574 540 KDYELKIGKYVDLLDMKAARIKKLEAQLRD 569
Cdd:COG4942 188 AALEALKAERQKLLARLEKELAELAAELAE 217
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
212-449 |
2.72e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 42.04 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 212 IDSQRGRIqELEHLSELLGSQL---RNKEKEIEESALHLKEQEAARQRSNiRDNVEMIKVRKQ-LAEKSSALAAMESKFL 287
Cdd:pfam05557 23 LEHKRARI-ELEKKASALKRQLdreSDRNQELQKRIRLLEKREAEAEEAL-REQAELNRLKKKyLEALNKKLNEKESQLA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 288 QLQENQRNFKT----------NHDV----LIAKSEELNVQLKEERSKCLHLEKELQSVAISKRRTEELEERVNDLERE-- 351
Cdd:pfam05557 101 DAREVISCLKNelselrrqiqRAELelqsTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEiq 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 352 -----KELLKENCDKLsSSVFSMTREQewklkeEQLKLQIAELETAIQSSLADKDEILGkLKVERDKKEKLMEENKDLQs 426
Cdd:pfam05557 181 sqeqdSEIVKNSKSEL-ARIPELEKEL------ERLREHNKHLNENIENKLLLKEEVED-LKRKLEREEKYREEAATLE- 251
|
250 260
....*....|....*....|...
gi 2024349574 427 cyLENKQQLDELKDYMKYLTKRC 449
Cdd:pfam05557 252 --LEKEKLEQELQSWVKLAQDTG 272
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
289-454 |
3.40e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 41.62 E-value: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 289 LQENQRNFKTNHDVLIAKSEELNVQLKEERSKCLHLEKELQSVAISK--RRTEELEERVNDLEREKELLKENCDKLSssv 366
Cdd:PRK12705 39 LQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERlvQKEEQLDARAEKLDNLENQLEEREKALS--- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 367 fsmTREQEWKLKEEQLKLQIaeLETAIQSSLADKDEILGKLKVERdKKEKLMEENKDLQSCYLENKQqldELKDYMKYLT 446
Cdd:PRK12705 116 ---ARELELEELEKQLDNEL--YRVAGLTPEQARKLLLKLLDAEL-EEEKAQRVKKIEEEADLEAER---KAQNILAQAM 186
|
....*...
gi 2024349574 447 KRCDVDVA 454
Cdd:PRK12705 187 QRIASETA 194
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
195-393 |
3.66e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 3.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 195 PNLLEDARAKIRNLETVIDSQRGRIQELEHLSELLGSQLRNKEKEIEE-------SALHLKEQEAARQRSNIR-----DN 262
Cdd:COG3206 211 SEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEllqspviQQLRAQLAELEAELAELSarytpNH 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 263 VEMIKVRKQLAEKSSALAAMESKFLQLQENQRnfktnhDVLIAKSEELNVQLKEerskclhLEKELQSVAiskrrteELE 342
Cdd:COG3206 291 PDVIALRAQIAALRAQLQQEAQRILASLEAEL------EALQAREASLQAQLAQ-------LEARLAELP-------ELE 350
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2024349574 343 ERVNDLEREKELLKENCDKLsssvfsMTREQEWKLKEEQLKLQIAELETAI 393
Cdd:COG3206 351 AELRRLEREVEVARELYESL------LQRLEEARLAEALTVGNVRVIDPAV 395
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
45-367 |
3.75e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.59 E-value: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 45 RKELEDKYLQLRDENI-SLKQHANKQEETIKRMATRLIQLvhDKKRNeqvgggpKRLGRTVKMEGMVEHLQERVRDLEKQ 123
Cdd:TIGR02169 778 EEALNDLEARLSHSRIpEIQAELSKLEEEVSRIEARLREI--EQKLN-------RLTLEKEYLEKEIQELQEQRIDLKEQ 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 124 NEilrskliSNKQQIHmpshrpiqykfaqprNSNGLKKASDAagtpEPTKKGMRLQNLEVRspplvlrrcgpnlLEDARA 203
Cdd:TIGR02169 849 IK-------SIEKEIE---------------NLNGKKEELEE----ELEELEAALRDLESR-------------LGDLKK 889
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 204 KIRNLETVIDSQRGRIQELehlsellgsqlrnkEKEIEESALHLKEQEAARQRSNIRdNVEMIKVRKQLAEKSSALAAME 283
Cdd:TIGR02169 890 ERDELEAQLRELERKIEEL--------------EAQIEKKRKRLSELKAKLEALEEE-LSEIEDPKGEDEEIPEEELSLE 954
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 284 SKFLQLQENQRNfktnhdvlIAKSEELNVqlkeerskclhleKELQSVAISKRRTEELEERVNDLEREKELLK---ENCD 360
Cdd:TIGR02169 955 DVQAELQRVEEE--------IRALEPVNM-------------LAIQEYEEVLKRLDELKEKRAKLEEERKAILeriEEYE 1013
|
....*..
gi 2024349574 361 KLSSSVF 367
Cdd:TIGR02169 1014 KKKREVF 1020
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
171-612 |
3.99e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.50 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 171 PTKKGMRLQNLEVRSPPLVLRRCGPNLLEDARAKIRNLETVIDSQRGRIQELE---HLSELLGSQLRNKEKEIEESALHL 247
Cdd:pfam02463 572 ELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVvegILKDTELTKLKESAKAKESGLRKG 651
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 248 KEQEAARQRSNiRDNVEMIKVRKQLAEKSsalaamESKFLQLQENQRNFKTNHDVLIAKSEelnvQLKEERSKCLHLEKE 327
Cdd:pfam02463 652 VSLEEGLAEKS-EVKASLSELTKELLEIQ------ELQEKAESELAKEEILRRQLEIKKKE----QREKEELKKLKLEAE 720
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 328 LQSvaISKRRTEELEERVNDLEREKELLKENCDKLSSSVFSMTREQEWKLKEEQLKLQIAELETAIQSSLADkdeilgkl 407
Cdd:pfam02463 721 ELL--ADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEE-------- 790
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 408 kvERDKKEKLMEEnkDLQSCYLENKQQLDELKdymkyltkrcdvDVAELSEALLLIKVRKEQKKNGDLICLEKDDDDIQK 487
Cdd:pfam02463 791 --EKEEKLKAQEE--ELRALEEELKEEAELLE------------EEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEE 854
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 488 VSERSMrKLQLAHAETVQELEKTRSMLIVQHKINKG--YQTEIEAVTQKMESLQKDYELKIGKYVDLLDMKaaRIKKLEA 565
Cdd:pfam02463 855 ELERLE-EEITKEELLQELLLKEEELEEQKLKDELEskEEKEKEEKKELEEESQKLNLLEEKENEIEERIK--EEAEILL 931
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2024349574 566 QLRDVaygSKRYKFRPEILPANPVNIFDETLHFERREGLFEIHISKV 612
Cdd:pfam02463 932 KYEEE---PEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKV 975
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
233-566 |
4.20e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.49 E-value: 4.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 233 LRNKEKEIEESALHLKEQEAARQRSNirdnveMIKVRKQLAEKSSALAAMESKFLQLQENQRNfKTNHDVLiakseelNV 312
Cdd:TIGR00618 158 LKAKSKEKKELLMNLFPLDQYTQLAL------MEFAKKKSLHGKAELLTLRSQLLTLCTPCMP-DTYHERK-------QV 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 313 QLKEERskclHLEKELQSVAISK---RRTEELEERVNDLEREKELLKENCDKLSSSVFSMTREQEwKLKEEQLKLQIAEL 389
Cdd:TIGR00618 224 LEKELK----HLREALQQTQQSHaylTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQE-RINRARKAAPLAAH 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 390 ETAIQSSLADKDEILGKLKVERDKKEKLMEENKDL--QSCYLENKQQL--------DELKDYMKYLTKRCDVDVAELSE- 458
Cdd:TIGR00618 299 IKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHvkQQSSIEEQRRLlqtlhsqeIHIRDAHEVATSIREISCQQHTLt 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 459 ----ALLLIKVRKEQKKNGDLICLEKDDDDIQKV----SERSMRKLQLAHAETVQELEKTRSMLIVQHkINKGYQTEIEA 530
Cdd:TIGR00618 379 qhihTLQQQKTTLTQKLQSLCKELDILQREQATIdtrtSAFRDLQGQLAHAKKQQELQQRYAELCAAA-ITCTAQCEKLE 457
|
330 340 350
....*....|....*....|....*....|....*..
gi 2024349574 531 VTQKMESLQKDYELKIG-KYVDLLDMKAARIKKLEAQ 566
Cdd:TIGR00618 458 KIHLQESAQSLKEREQQlQTKEQIHLQETRKKAVVLA 494
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
197-481 |
4.53e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.50 E-value: 4.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 197 LLEDARAKIRNLETVIDSQRGRIQELEHLSELLGSQLRNKEKEIEESALHLKEQEAARQrsnirdnvEMIKVRKQLAEKS 276
Cdd:pfam02463 294 EEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKRE--------AEEEEEEELEKLQ 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 277 SALAAMESKFLQLQENQRNFKTNHDVLIAKSEELNVQLKEERSKCLHLEKELQSVA-----ISKRRTEELEERVNDLERE 351
Cdd:pfam02463 366 EKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLkeekkEELEILEEEEESIELKQGK 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 352 KELLKENCDKLSS---SVFSMTREQEWKLKEEQLKLQIAELETAIQSSLADKDEILGKLKVER-DKKEKLMEENKDLQSC 427
Cdd:pfam02463 446 LTEEKEELEKQELkllKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGlKVLLALIKDGVGGRII 525
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2024349574 428 YLENKQQLDELKDyMKYLTKRCDVDVAELSEALLLIKVRKEQKKNGDLICLEKD 481
Cdd:pfam02463 526 SAHGRLGDLGVAV-ENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGAR 578
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
339-443 |
4.55e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.22 E-value: 4.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 339 EELEERVNDLEREKELLKENCDKLSSSvfsmtREQEWKLKEEQLKLQIAELETAIQSSLADKDEILGKLKVERDKKEKLM 418
Cdd:COG0542 414 DELERRLEQLEIEKEALKKEQDEASFE-----RLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIP 488
|
90 100
....*....|....*....|....*
gi 2024349574 419 EENKDLQscylENKQQLDELKDYMK 443
Cdd:COG0542 489 ELEKELA----ELEEELAELAPLLR 509
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
247-465 |
6.36e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 6.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 247 LKEQEAARQRSNIRDNVEMIKVRKQLAEKSSALAAMESKFLQLQENQRNfktnhdvLIAKSEELNVQLKEERSKCLHLEK 326
Cdd:COG4717 51 LEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEE-------LEEELEELEAELEELREELEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 327 ELQSVAISKRRtEELEERVNDLEREKELLKENcdklsssvfsMTREQEWKLKEEQLKLQIAELETAIQSSLADKD-EILG 405
Cdd:COG4717 124 LLQLLPLYQEL-EALEAELAELPERLEELEER----------LEELRELEEELEELEAELAELQEELEELLEQLSlATEE 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024349574 406 KLKVERDKKEKLMEENKDLQSCYLENKQQLDELKDYMKYL--TKRCDVDVAELSEALLLIKV 465
Cdd:COG4717 193 ELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLenELEAAALEERLKEARLLLLI 254
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
264-569 |
6.43e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.93 E-value: 6.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 264 EMIKVRKQLAEKSSALAAMESKFLQLQEN----QRNFKTNHDvLIAKSEELNVQL---KEERSKCLHlekELQSvaiskr 336
Cdd:pfam01576 13 ELQKVKERQQKAESELKELEKKHQQLCEEknalQEQLQAETE-LCAEAEEMRARLaarKQELEEILH---ELES------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 337 RTEELEERVNDLEREKELLKENCDKLsssvfsmtreqEWKLKEEQLKLQIAELETAIQSSLADK--DEILgklkVERDKK 414
Cdd:pfam01576 83 RLEEEEERSQQLQNEKKKMQQHIQDL-----------EEQLDEEEAARQKLQLEKVTTEAKIKKleEDIL----LLEDQN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 415 EKLMEENKDLQSCYLENKQQLDELKDYMKYLTKRCDVDVAELSEalLLIKVRKEQKKNGDLiclekddDDIQKVSERSMR 494
Cdd:pfam01576 148 SKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISD--LEERLKKEEKGRQEL-------EKAKRKLEGEST 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024349574 495 KLQLAHAETVQELEKTRSMLIVQHKINKGYQTEIE-AVTQKMESLQKDYELKIGK---YVDLLDMKAARiKKLEAQLRD 569
Cdd:pfam01576 219 DLQEQIAELQAQIAELRAQLAKKEEELQAALARLEeETAQKNNALKKIRELEAQIselQEDLESERAAR-NKAEKQRRD 296
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
268-420 |
8.63e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.15 E-value: 8.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 268 VRKQLAEKSSALAAMESKFLqLQENQRNFKTNHD--VLIAKSEELNVQ------LKEERSKCLHLEKELQsvaiskRRTE 339
Cdd:PRK12704 24 VRKKIAEAKIKEAEEEAKRI-LEEAKKEAEAIKKeaLLEAKEEIHKLRnefekeLRERRNELQKLEKRLL------QKEE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349574 340 ELEERVNDLEREKELLKEncdklsssvfsmtREQEWKLKEEQLKLQIAELETAIQSSLADKDEILGkLKVErDKKEKLME 419
Cdd:PRK12704 97 NLDRKLELLEKREEELEK-------------KEKELEQKQQELEKKEEELEELIEEQLQELERISG-LTAE-EAKEILLE 161
|
.
gi 2024349574 420 E 420
Cdd:PRK12704 162 K 162
|
|
| |
