|
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 ... |
547-688 |
4.08e-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: 4.08e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 547 TLHFERREGLFEIHISKVIFSSEAVHAFGDHEPATFCTYAFYDFELQATPVLHGHTLSYDFTSQYLAQIDDSFLHYIQSN 626
Cdd:pfam11618 1 TVELERGENLFELHIGGVTFSPEALRALGDKEPSTFCTYDFYDFETQTTPVVRGLNPFYDFTSQYKVTVDDLFLQYLQTN 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024349576 627 SVTLEVHHAYGTDYETVATCQLALHEVLEQ-NGRIYSTAVLVGINGNIQDFGTVEYWVRLQAP 688
Cdd:pfam11618 81 SLTLELHQALGVDFKTLAAAQLRLHGLLEDrGGRIHGTVTLTGVEGEIQIIGTLEYWIRLRVP 143
|
|
| RPGR1_C |
pfam18111 |
Retinitis pigmentosa G-protein regulator interacting C-terminal; This is the C-terminal domain ... |
1052-1215 |
6.92e-57 |
|
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: 194.17 E-value: 6.92e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 1052 ATEKIRIEIISLGLT-ESRIVEDNTIQQLFVECRLYNFIAE--ETPVSLPKPPCGQRVHYNYSNVIHVDKANNRARREYL 1128
Cdd:pfam18111 1 DSDTIRIEIISLQLLnESEVMQDDNIQQLFVEYRFLGRPEEetETPVSLPKPKTGQELYYNFSKVIDVDKEKNSARREIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 1129 KSILQKPSLRTDRLLFTVVSDPPeDEQDLECEDIGFAYVSLREIFEKKRDVIEQDIFVFDSQDDSAVIGKLRVTVEALHA 1208
Cdd:pfam18111 81 RSMLLPEDPNQGNLKFTVVSEPL-DTEDGECEEIGYAYVDLKQILQSGRDIIEQDLDVKDARDENEQIGKLKVSVEALAA 159
|
....*..
gi 2024349576 1209 LCSVYEE 1215
Cdd:pfam18111 160 LRAIYSE 166
|
|
| C2 |
cd00030 |
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ... |
739-834 |
8.03e-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: 65.55 E-value: 8.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 739 LHVTIKCCNRLQSQKKHLQPNSYVVYKFFDFAHHDTRIIPSSSNPQIDDHMCFQVPMTADldqylkwESLTFYVFDDSEM 818
Cdd:cd00030 1 LRVTVIEARNLPAKDLNGKSDPYVKVSLGGKQKFKTKVVKNTLNPVWNETFEFPVLDPES-------DTLTVEVWDKDRF 73
|
90
....*....|....*.
gi 2024349576 819 GEDGFLGKANVPLIPL 834
Cdd:cd00030 74 SKDDFLGEVEIPLSEL 89
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
99-449 |
1.17e-09 |
|
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: 63.15 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 99 RLGRTVKMEgmveHLQERVRDLEKQNEILRSKLISNKQQIhmpshrpiqykfaqprnSNGLKKASDAAGTPEPTKKGMRL 178
Cdd:TIGR02168 672 ILERRREIE----ELEEKIEELEEKIAELEKALAELRKEL-----------------EELEEELEQLRKELEELSRQISA 730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 179 QNLEVRSpplvLRRCGPNLLEDARAKIRNLSNIRDnvEMIKVRKQLAEKSSALAAMESKFLQLQENQRNFKTNHDVLIAK 258
Cdd:TIGR02168 731 LRKDLAR----LEAEVEQLEERIAQLSKELTELEA--EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREA 804
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 259 SEELNVQLKEERSKCLHLEKELQSvaiSKRRTEELEERVNDLEREKELLKENCDKLSSSVfsmtreqewklkeEQLKLQI 338
Cdd:TIGR02168 805 LDELRAELTLLNEEAANLRERLES---LERRIAATERRLEDLEEQIEELSEDIESLAAEI-------------EELEELI 868
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 339 AELETAIQSSLADKDEILGKLKVERDKKEKLMEENKDLQSCYLENKQQLDELKDYMKYLTKRCdvDVAELSEALLLIKVR 418
Cdd:TIGR02168 869 EELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRL--EGLEVRIDNLQERLS 946
|
330 340 350
....*....|....*....|....*....|...
gi 2024349576 419 KEQKKNGDLI--CLEKDDDDIQKVsERSMRKLQ 449
Cdd:TIGR02168 947 EEYSLTLEEAeaLENKIEDDEEEA-RRRLKRLE 978
|
|
| C2 |
pfam00168 |
C2 domain; |
739-846 |
2.37e-09 |
|
C2 domain;
Pssm-ID: 425499 [Multi-domain] Cd Length: 104 Bit Score: 55.79 E-value: 2.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 739 LHVTIKCCNRLQSQKKHLQPNSYVVYKFFDFAH-HDTRIIPSSSNPQIDDHMCFQVPMTADldqylkwESLTFYVFDDSE 817
Cdd:pfam00168 3 LTVTVIEAKNLPPKDGNGTSDPYVKVYLLDGKQkKKTKVVKNTLNPVWNETFTFSVPDPEN-------AVLEIEVYDYDR 75
|
90 100
....*....|....*....|....*....
gi 2024349576 818 MGEDGFLGKANVPLIPLACNRSISGTFEV 846
Cdd:pfam00168 76 FGRDDFIGEVRIPLSELDSGEGLDGWYPL 104
|
|
| C2 |
smart00239 |
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ... |
739-831 |
3.20e-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: 3.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 739 LHVTIKCCNRLQSQKKHLQPNSYVVYKFFDFAHHD--TRIIPSSSNPQIDDHMCFQVPMTADldqylkwESLTFYVFDDS 816
Cdd:smart00239 2 LTVKIISARNLPPKDKGGKSDPYVKVSLDGDPKEKkkTKVVKNTLNPVWNETFEFEVPPPEL-------AELEIEVYDKD 74
|
90
....*....|....*
gi 2024349576 817 EMGEDGFLGKANVPL 831
Cdd:smart00239 75 RFGRDDFIGQVTIPL 89
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
198-495 |
3.13e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.07 E-value: 3.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 198 LEDARAKIRnLSNIRDNVEMIK-VRKQLAEKSSALAAMESkflQLQENQRNFKTNHDVLiaksEELNVQLKEERS-KCLH 275
Cdd:TIGR02169 220 KREYEGYEL-LKEKEALERQKEaIERQLASLEEELEKLTE---EISELEKRLEEIEQLL----EELNKKIKDLGEeEQLR 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 276 LEKELQSVAISKRRTE----ELEERVNDLEREKELLKENCDKLSSSVFSMTRE-QEWKLKEEQLKLQIAELETAIQSSLA 350
Cdd:TIGR02169 292 VKEKIGELEAEIASLErsiaEKERELEDAEERLAKLEAEIDKLLAEIEELEREiEEERKRRDKLTEEYAELKEELEDLRA 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 351 DKDEILGKLKVERDKKEKLMEENKDLQSCYLENKQQLDELKDymkyLTKRCDVDVAELSEALllikVRKEQKKNGdlicL 430
Cdd:TIGR02169 372 ELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQE----ELQRLSEELADLNAAI----AGIEAKINE----L 439
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024349576 431 EKDDDDIQKVSERSMRKLQlahaETVQELEKTRSMLivqhkinKGYQTEIEAVTQKMESLQKDYE 495
Cdd:TIGR02169 440 EEEKEDKALEIKKQEWKLE----QLAADLSKYEQEL-------YDLKEEYDRVEKELSKLQRELA 493
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
105-522 |
1.11e-06 |
|
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: 53.20 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 105 KMEGMVEHLQERVRDLEKQNEILRSKlISNKQQIHMPSH--RPIQYKFAQPRNSNGL-KKASDAAGTPEPTKKGMRLQNL 181
Cdd:pfam15921 228 ELDTEISYLKGRIFPVEDQLEALKSE-SQNKIELLLQQHqdRIEQLISEHEVEITGLtEKASSARSQANSIQSQLEIIQE 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 182 EVRSPPLVLRRCGPNL---LEDARAKIRNLSNI-RDNVEmiKVRKQLAEKSSALAAMESKFLQLQENQRNFKTNHDVLIA 257
Cdd:pfam15921 307 QARNQNSMYMRQLSDLestVSQLRSELREAKRMyEDKIE--ELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLA 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 258 K--SEELNVQLKEERSKCLHLEKELQSVAISKRRtEELEERVNDLEREKELLKencdklsssvfSMTREQEWKLKEE--- 332
Cdd:pfam15921 385 DlhKREKELSLEKEQNKRLWDRDTGNSITIDHLR-RELDDRNMEVQRLEALLK-----------AMKSECQGQMERQmaa 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 333 -QLKLQIAELETAIQSSLADKDEILGKLKVERDKKEKLMEENK----DLQSCYLENKQQLDELKDYMKYLTKRCDVDVAE 407
Cdd:pfam15921 453 iQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSErtvsDLTASLQEKERAIEATNAEITKLRSRVDLKLQE 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 408 LSEalllikvrkeqkkngdlicLEKDDDDIQKV-SERSMRKLQLAHAETVQELEKTR----SMLIVQHKINKGyqtEIEA 482
Cdd:pfam15921 533 LQH-------------------LKNEGDHLRNVqTECEALKLQMAEKDKVIEILRQQienmTQLVGQHGRTAG---AMQV 590
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2024349576 483 VTQKMESLQKDYELKIGKYVDLLDMKAARIKKLEAQLRDV 522
Cdd:pfam15921 591 EKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDL 630
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
219-492 |
1.14e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.14 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 219 KVRKQLAEKSSALaameSKFLQLQEN-QRNFKTNHDVLIAKSEELNVQLKEERSkclhLEKELQSVAISKRRTEELEERV 297
Cdd:PRK03918 169 EVIKEIKRRIERL----EKFIKRTENiEELIKEKEKELEEVLREINEISSELPE----LREELEKLEKEVKELEELKEEI 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 298 NDLEREKELLKENCDKLSSSVFSM-TREQEWKLKEEQLKLQIAELETAiqSSLADKDEILGKLKVE-RDKKEKLMEENKD 375
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRELeERIEELKKEIEELEEKVKELKEL--KEKAEEYIKLSEFYEEyLDELREIEKRLSR 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 376 LQSCYLENKQQLDELKDymkyltkrcdvDVAELSEallLIKVRKEQKKngDLICLEKDDDDIQKVSERSMRKLQLAHAET 455
Cdd:PRK03918 319 LEEEINGIEERIKELEE-----------KEERLEE---LKKKLKELEK--RLEELEERHELYEEAKAKKEELERLKKRLT 382
|
250 260 270
....*....|....*....|....*....|....*..
gi 2024349576 456 VQELEKTRSMLIVQHKINKGYQTEIEAVTQKMESLQK 492
Cdd:PRK03918 383 GLTPEKLEKELEELEKAKEEIEEEISKITARIGELKK 419
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
196-516 |
1.39e-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: 52.72 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 196 NLLEDARAKIRNLSNirdnvEMIKVRKQLAEKSSALAAMESKFLQLQENQRNFKTNHDVLIAKSE-----ELNVQLKEER 270
Cdd:TIGR04523 246 TEISNTQTQLNQLKD-----EQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEqdwnkELKSELKNQE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 271 SKCLHLEKEL----QSVAISKRRTEELEERVNDLEREKELLKENCDKLSSSVFSMTREQEWKLKE-EQLKLQIAELETAI 345
Cdd:TIGR04523 321 KKLEEIQNQIsqnnKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEiKNLESQINDLESKI 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 346 QSSLADKDEILGKLKVERDKKEKLMEENKDLQSCYLENKQQLDELKD-------YMKYLTKRCDVDVAELSEALLLIK-V 417
Cdd:TIGR04523 401 QNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNqdsvkelIIKNLDNTRESLETQLKVLSRSINkI 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 418 RKEQKKNGDLIclekdDDDIQKVSERSMRKLQLahAETVQELEKTRSMLIVQHKINKGYQTEIEAVTQKMES--LQKDYE 495
Cdd:TIGR04523 481 KQNLEQKQKEL-----KSKEKELKKLNEEKKEL--EEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDelNKDDFE 553
|
330 340
....*....|....*....|.
gi 2024349576 496 LKIGKYVDLLDMKAARIKKLE 516
Cdd:TIGR04523 554 LKKENLEKEIDEKNKEIEELK 574
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
219-522 |
1.82e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.37 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 219 KVRKQLAEKssalaameskflQLQENQRNFKTNHDVLiaksEELNVQLKeerskclHLEKELQSVAISKRRTEELEE--- 295
Cdd:TIGR02168 171 KERRKETER------------KLERTRENLDRLEDIL----NELERQLK-------SLERQAEKAERYKELKAELRElel 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 296 -----RVNDLEREKELLKENCDKLSSSVFSMTRE-QEWKLKEEQLKLQIAELETAI-------QSSLADKDEILGKLKVE 362
Cdd:TIGR02168 228 allvlRLEELREELEELQEELKEAEEELEELTAElQELEEKLEELRLEVSELEEEIeelqkelYALANEISRLEQQKQIL 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 363 RDKKEKLMEENKDLQSCYLENKQQLDELKDYMKYLTKRCDVDVAELSEALLLIKVRKEQKKNGDLICLEKDDDDIQKVSE 442
Cdd:TIGR02168 308 RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 443 RSMRKLQLA-HAETVQELEKTRSMLIVQHKINkgyQTEIEAVTQKMESLQKDyELKIGkyvdlLDMKAARIKKLEAQLRD 521
Cdd:TIGR02168 388 VAQLELQIAsLNNEIERLEARLERLEDRRERL---QQEIEELLKKLEEAELK-ELQAE-----LEELEEELEELQEELER 458
|
.
gi 2024349576 522 V 522
Cdd:TIGR02168 459 L 459
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
221-516 |
3.02e-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: 51.61 E-value: 3.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 221 RKQLAEKSSALAAMESKFLQLQENQRNFKTNHDVLIAKSEELNVQLKEERSKCLHLEKELQSVaisKRRTEELEERVNDL 300
Cdd:TIGR02169 673 PAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKL---KERLEELEEDLSSL 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 301 EREKELLKENCDKLSSsvfsmtREQEWKLKEEQLKLQIAELETAI-QSSLADKDEILGKLKVERDKKEKLMEE-NKDLQS 378
Cdd:TIGR02169 750 EQEIENVKSELKELEA------RIEELEEDLHKLEEALNDLEARLsHSRIPEIQAELSKLEEEVSRIEARLREiEQKLNR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 379 CYLEnKQQLDELKDYMKYLTKRCDVDVAELSEALLLIKVRKEQKK-------------NGDLICLEKDDDDIQKVSERSM 445
Cdd:TIGR02169 824 LTLE-KEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEeeleeleaalrdlESRLGDLKKERDELEAQLRELE 902
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024349576 446 RKLQLAHAEtVQELEKTRSMLIVQHKINKGYQTEIEAVTQKMESLQKDyELKIGKYVDLLDMKAARIKKLE 516
Cdd:TIGR02169 903 RKIEELEAQ-IEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEE-ELSLEDVQAELQRVEEEIRALE 971
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
257-519 |
3.81e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.60 E-value: 3.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 257 AKSEELNVQLKEERSKCLHLEKELQSVaisKRRTEELEERVNDLEREKELLKENCDKLSSSVFSMTREQE-WKLKEEQLK 335
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAEL---RKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEqLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 336 LQIAELETAIQSSLADKDEILGKLKVERDKKEKLMEENKDLQSCYLENKQQLDELKDymkyltkrcdvDVAELSEALLLI 415
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA-----------ELTLLNEEAANL 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 416 KVRKEQKKNgDLICLEKDDDDIQKVSER---SMRKLQLAHAETVQELEKTRSMLIVQHKINKGYQTEIEAVTQKMESLQ- 491
Cdd:TIGR02168 823 RERLESLER-RIAATERRLEDLEEQIEElseDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSe 901
|
250 260 270
....*....|....*....|....*....|
gi 2024349576 492 --KDYELKIGKYVDLLDMKAARIKKLEAQL 519
Cdd:TIGR02168 902 elRELESKRSELRRELEELREKLAQLELRL 931
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
198-522 |
7.12e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 7.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 198 LEDARAKIRNLSNIRDNVEMIKVRKQLAEKSsaLAAMESKFLQLQENQRNFKTNHDVL---------IAKSEELNVQLKE 268
Cdd:PRK03918 223 LEKLEKEVKELEELKEEIEELEKELESLEGS--KRKLEEKIRELEERIEELKKEIEELeekvkelkeLKEKAEEYIKLSE 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 269 ERSKCL----HLEKELQSVaisKRRTEELEERVNDLEREKELLKENCDKLSSSVFSMTREQEWKLKEEQLKLQIAELETa 344
Cdd:PRK03918 301 FYEEYLdelrEIEKRLSRL---EEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELER- 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 345 IQSSLADK--DEILGKLKVERDKKEKLMEENKDLQSCYLENKQQLDELKDYMKYLTK---RCDVDVAELSEalllikvrk 419
Cdd:PRK03918 377 LKKRLTGLtpEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgKCPVCGRELTE--------- 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 420 EQKKNgdliCLEKDDDDIQKVSERsMRKLQLAHAETVQELEKTRSMLIVQHKINKGYQT--EIEAVTQKM-----ESLQK 492
Cdd:PRK03918 448 EHRKE----LLEEYTAELKRIEKE-LKEIEEKERKLRKELRELEKVLKKESELIKLKELaeQLKELEEKLkkynlEELEK 522
|
330 340 350
....*....|....*....|....*....|....*....
gi 2024349576 493 DYE---------LKIGKYVDLLDMKAARIKKLEAQLRDV 522
Cdd:PRK03918 523 KAEeyeklkeklIKLKGEIKSLKKELEKLEELKKKLAEL 561
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
198-428 |
8.02e-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: 8.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 198 LEDARAKIRNL--SNIRDNVEMIKVRKQLAEKSSALAAMESKFLQLQENQRNFKTNHDVLIAKSEELN-------VQLKE 268
Cdd:TIGR02168 304 KQILRERLANLerQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELEsrleeleEQLET 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 269 ERSKCLHLEKELQSvaISKRRtEELEERVNDLEREKELLKENcdklsssvfsmTREQEWKLKEEQLKlqiaeletAIQSS 348
Cdd:TIGR02168 384 LRSKVAQLELQIAS--LNNEI-ERLEARLERLEDRRERLQQE-----------IEELLKKLEEAELK--------ELQAE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 349 LADKDEILGKLKVERDKKEKLMEEnkdLQSCYLENKQQLDELKDYMKYLTKRCDVDVAELSEALLLIKVRKEQKKNGDLI 428
Cdd:TIGR02168 442 LEELEEELEELQEELERLEEALEE---LREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGL 518
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
289-492 |
1.69e-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: 48.74 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 289 RTEELEERVNDLEREKELLKENCDKLSSSvfSMTREQEWKLKEEQLKLQIAELETAIQSSLADKDEILGKLKVERDKKEK 368
Cdd:pfam07888 35 RLEECLQERAELLQAQEAANRQREKEKER--YKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 369 LMEENKDLQSCYLENKQQLDELKDYMKYLTKRCDVDVAELSeallliKVRKEQKKngdLICLEKDDDDIQKVSERSMRKL 448
Cdd:pfam07888 113 LSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELE------RMKERAKK---AGAQRKEEEAERKQLQAKLQQT 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2024349576 449 QLAHAETVQELEKTRSMLIVQHKINKGYQTEIEAVTQKMESLQK 492
Cdd:pfam07888 184 EEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHR 227
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
266-521 |
2.35e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 48.77 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 266 LKEERSKC---LHlekELQSVAISKRRTEELEERVNDLEREKELLKENCDKLSSSVfsmtrEQEWKLKEEQLKLQIAELE 342
Cdd:PRK05771 14 LKSYKDEVleaLH---ELGVVHIEDLKEELSNERLRKLRSLLTKLSEALDKLRSYL-----PKLNPLREEKKKVSVKSLE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 343 TAIQSSLADKDEILGKLKVERDKKEKLMEENKDLQScyleNKQQLDELKDY---MKYLTKRCDVDV------AELSEALL 413
Cdd:PRK05771 86 ELIKDVEEELEKIEKEIKELEEEISELENEIKELEQ----EIERLEPWGNFdldLSLLLGFKYVSVfvgtvpEDKLEELK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 414 LIKVRK-----EQKKNGD---LICLEKDDDDIQKVSER-SMRKLQLAHAETVQE-LEKTRSMLIvqhKINKgyqtEIEAV 483
Cdd:PRK05771 162 LESDVEnveyiSTDKGYVyvvVVVLKELSDEVEEELKKlGFERLELEEEGTPSElIREIKEELE---EIEK----ERESL 234
|
250 260 270
....*....|....*....|....*....|....*...
gi 2024349576 484 TQKMESLQKDYELKIGKYVDLLDMKAARIKKLEAQLRD 521
Cdd:PRK05771 235 LEELKELAKKYLEELLALYEYLEIELERAEALSKFLKT 272
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
201-501 |
3.27e-05 |
|
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: 48.20 E-value: 3.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 201 ARAKIRNLSNIRD---NVEMIKVRKQ-LAEKSSALAAMESkfLQLQENQRNFKTNHDVLIAKSEELnvqLKEERSKCLHl 276
Cdd:pfam17380 343 AMERERELERIRQeerKRELERIRQEeIAMEISRMRELER--LQMERQQKNERVRQELEAARKVKI---LEEERQRKIQ- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 277 EKELQSVAISKRRTEELEERVNDLEREKEllkencdklsssvfsmtREQEwKLKEEQLKLQiAELETAIQSSLADKDEIL 356
Cdd:pfam17380 417 QQKVEMEQIRAEQEEARQREVRRLEEERA-----------------REME-RVRLEEQERQ-QQVERLRQQEEERKRKKL 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 357 GKLKVERDKKEKLMEENKDLQSCYLENKQQLDELKDYMKYLTKRCDVDVAELSEALLLIKVRKEQKKNGDLICLEKDDDD 436
Cdd:pfam17380 478 ELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQ 557
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024349576 437 IQKVSERSMRklqlahaetVQELEKTRSMLiVQHKINKGYQTEIEAVTQkMESLQKDYELKIGKY 501
Cdd:pfam17380 558 MRKATEERSR---------LEAMEREREMM-RQIVESEKARAEYEATTP-ITTIKPIYRPRISEY 611
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
198-498 |
4.13e-05 |
|
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: 47.79 E-value: 4.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 198 LEDARAKIRNLSNIRDN--VEMIKVRKQLAEKSSALaameskflqlqENQRNFKTNHDVLIAKSEELNVQLKEERSKCLH 275
Cdd:pfam05483 386 LQKKSSELEEMTKFKNNkeVELEELKKILAEDEKLL-----------DEKKQFEKIAEELKGKEQELIFLLQAREKEIHD 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 276 LEKELQSVAISKRR-TEELEERVNDLEREK---ELLKENCDKLSSSVFSMTREQEwklkeeQLKLQIAELETAIQSSLAD 351
Cdd:pfam05483 455 LEIQLTAIKTSEEHyLKEVEDLKTELEKEKlknIELTAHCDKLLLENKELTQEAS------DMTLELKKHQEDIINCKKQ 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 352 KDEILGKLKVERDKKEKLMEEnkdLQSCYLENKQQLDELKdymkyltkrCDVDVAELSEALLLIKVRKEQKKngdLICLE 431
Cdd:pfam05483 529 EERMLKQIENLEEKEMNLRDE---LESVREEFIQKGDEVK---------CKLDKSEENARSIEYEVLKKEKQ---MKILE 593
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024349576 432 KDDDDIQKVSERSMRKLQLAHAETvQELEK-----TRSMLIVQHKINKgYQTEIEAVTQKMESLQKDYELKI 498
Cdd:pfam05483 594 NKCNNLKKQIENKNKNIEELHQEN-KALKKkgsaeNKQLNAYEIKVNK-LELELASAKQKFEEIIDNYQKEI 663
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
198-460 |
4.71e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.01 E-value: 4.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 198 LEDARAKIRNLSN--IRDNVEMIKVRKQLAEKSSALAAMESKFLQLQENQRNFKT-------NHDVLIAKSEELNVQLKE 268
Cdd:COG1196 241 LEELEAELEELEAelEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAelarleqDIARLEERRRELEERLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 269 ERSKCLHLEKELQSVaisKRRTEELEERVNDLEREKELLKENCDKLSSSVFSMTRE-QEWKLKEEQLKLQIAELETAIQS 347
Cdd:COG1196 321 LEEELAELEEELEEL---EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAElAEAEEELEELAEELLEALRAAAE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 348 SLADKDEILGKLKVERDKKEKLMEENKDLQSCYLENKQQLDELKDymkyLTKRCDVDVAELSEALLLIKVRKEQKKNGDL 427
Cdd:COG1196 398 LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE----ALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
250 260 270
....*....|....*....|....*....|...
gi 2024349576 428 ICLEKDDDDIQKVSERSMRKLQLAHAETVQELE 460
Cdd:COG1196 474 LLEAALAELLEELAEAAARLLLLLEAEADYEGF 506
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
119-375 |
5.83e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 47.59 E-value: 5.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 119 DLEKQNEILRSKLISNKQQIHMPSHRPIQYKFAQPRNSNGLKKASDAAGTPEPTKKGMRLQNLEVRSPPLVLRrcgpnll 198
Cdd:PLN02939 167 ALQGKINILEMRLSETDARIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLK------- 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 199 EDARAKIRNLSNIRDNVE-MIKVRKQLAEKSSALAAMESKFLQLQENQRNFKT-NHDVLIAKSEELNVQLKEerskclhL 276
Cdd:PLN02939 240 DDIQFLKAELIEVAETEErVFKLEKERSLLDASLRELESKFIVAQEDVSKLSPlQYDCWWEKVENLQDLLDR-------A 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 277 EKELQSVAISKRRTEELEERVNDLErekELLKE-NCDKLSSSVFSMTrEQEWKLKEEQLKLQIAELETAI---QSSLADK 352
Cdd:PLN02939 313 TNQVEKAALVLDQNQDLRDKVDKLE---ASLKEaNVSKFSSYKVELL-QQKLKLLEERLQASDHEIHSYIqlyQESIKEF 388
|
250 260
....*....|....*....|...
gi 2024349576 353 DEILGKLKVERDKKEklMEENKD 375
Cdd:PLN02939 389 QDTLSKLKEESKKRS--LEHPAD 409
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
20-367 |
5.91e-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: 47.42 E-value: 5.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 20 TLPRVRGLLASARNVKA--RQAVSQFSRKE--LEDKYLQLRDENISLKQHANKQEET---IKRMATR----LIQLVHDKK 88
Cdd:pfam15921 459 SLEKVSSLTAQLESTKEmlRKVVEELTAKKmtLESSERTVSDLTASLQEKERAIEATnaeITKLRSRvdlkLQELQHLKN 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 89 RNEQVgggpkrlgRTVKMEgmVEHLQERVRDLEKQNEILRSKlISNKQQI---HMPSHRPIQYKFAQPRNSNGLKKASDA 165
Cdd:pfam15921 539 EGDHL--------RNVQTE--CEALKLQMAEKDKVIEILRQQ-IENMTQLvgqHGRTAGAMQVEKAQLEKEINDRRLELQ 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 166 AGTPEPTKKGMRLQNLEVRSPPLVLRRCgpNLLEDARAKIRNLSNIRDnvEMIKVRKQLAEKSSALAAMESKFLQLQenq 245
Cdd:pfam15921 608 EFKILKDKKDAKIRELEARVSDLELEKV--KLVNAGSERLRAVKDIKQ--ERDQLLNEVKTSRNELNSLSEDYEVLK--- 680
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 246 RNFKTNHDVLIAKSEELNVQLKEERSKCLHLEKELQS----------VAI-------SKR--------RTEELEERVNDL 300
Cdd:pfam15921 681 RNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSmegsdghamkVAMgmqkqitAKRgqidalqsKIQFLEEAMTNA 760
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 301 EREKELLKENCDKLSSSV-------------FSMTREQEWKLKE---------EQLKLQIAELETAIQSSlaDKDEILGK 358
Cdd:pfam15921 761 NKEKHFLKEEKNKLSQELstvateknkmageLEVLRSQERRLKEkvanmevalDKASLQFAECQDIIQRQ--EQESVRLK 838
|
....*....
gi 2024349576 359 LKVERDKKE 367
Cdd:pfam15921 839 LQHTLDVKE 847
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
210-392 |
6.62e-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: 47.32 E-value: 6.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 210 NIRDNVEmiKVRKQLAEKSSALAAMESKFLQLQENQRNFKTNHDVLIAKSEELNVQLKEERSKCLHLEKELQSVAISKRR 289
Cdd:TIGR04523 479 KIKQNLE--QKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKK 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 290 tEELEERVNDLEREKELLKENCDKLSSSVFSMtrEQEWKLKEEQLKLQIAELETAIQSsladKDEILGKLKVERDKKEKL 369
Cdd:TIGR04523 557 -ENLEKEIDEKNKEIEELKQTQKSLKKKQEEK--QELIDQKEKEKKDLIKEIEEKEKK----ISSLEKELEKAKKENEKL 629
|
170 180
....*....|....*....|...
gi 2024349576 370 MEENKDLQSCYLENKQQLDELKD 392
Cdd:TIGR04523 630 SSIIKNIKSKKNKLKQEVKQIKE 652
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
199-575 |
1.03e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.05 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 199 EDARAKIRNLSNIRDNVEmiKVRKQLAEKSSALAAMESKFLQLQENQrnfktnhDVLIAKSEELNVQLKEERSKCLHLEK 278
Cdd:COG4372 31 EQLRKALFELDKLQEELE--QLREELEQAREELEQLEEELEQARSEL-------EQLEEELEELNEQLQAAQAELAQAQE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 279 ELQSVaisKRRTEELEERVNDLEREKELLKEncdklsssvfsmtreqewklKEEQLKLQIAELETAIQSSLADKDEILGK 358
Cdd:COG4372 102 ELESL---QEEAEELQEELEELQKERQDLEQ--------------------QRKQLEAQIAELQSEIAEREEELKELEEQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 359 LKVERDKKEKLMEENKdlqscYLENKQQLDELKDYMKYLTKRCDVDVAELSEALLLIKVRKEQKKNGDLICLEKDDDDIQ 438
Cdd:COG4372 159 LESLQEELAALEQELQ-----ALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 439 KVSERSMRKLQLAHAETVQELEKTRSMLIVQHKINKGYQTEIEAVTQKMESLQKDYELKIGKYVDLLDMKAARIKKLEAQ 518
Cdd:COG4372 234 ALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGAL 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2024349576 519 LRDVAYGSKRYKFRPEILPANPVNIFDETLHFERREGLFEIHISKVIFSSEAVHAFG 575
Cdd:COG4372 314 EDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
198-423 |
1.06e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 198 LEDARAKIRNLSNIRD-NVEMIKVRKQLAEKSSALAAMESKFLQ-----LQENQRNFKTNHDVLIAKSEELNVQLKEERS 271
Cdd:COG4913 244 LEDAREQIELLEPIRElAERYAAARERLAELEYLRAALRLWFAQrrlelLEAELEELRAELARLEAELERLEARLDALRE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 272 KCLHLEKELQSvaISKRRTEELEERVNDLEREKELLKENCDKLSSSVFSM-----TREQEWKLKEEQLKLQIAELETAIQ 346
Cdd:COG4913 324 ELDELEAQIRG--NGGDRLEQLEREIERLERELEERERRRARLEALLAALglplpASAEEFAALRAEAAALLEALEEELE 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 347 SSLADKDEILGKLKVERDKKEKLMEENKDLQScyleNK----QQLDELKDYMKyltKRCDVDVAELSEALLLIKVRKEQK 422
Cdd:COG4913 402 ALEEALAEAEAALRDLRRELRELEAEIASLER----RKsnipARLLALRDALA---EALGLDEAELPFVGELIEVRPEEE 474
|
.
gi 2024349576 423 K 423
Cdd:COG4913 475 R 475
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
44-492 |
2.00e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 44 SRKELEDKYLQLRDENISLKQHANKQEETIKRM------ATRLIQLVHDK-KRNEQVGGGPKRLGRtvkMEGMVEHLQER 116
Cdd:PRK03918 253 SKRKLEEKIRELEERIEELKKEIEELEEKVKELkelkekAEEYIKLSEFYeEYLDELREIEKRLSR---LEEEINGIEER 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 117 VRDLEKQNEIL-----RSKLISNKQQIHMPSHRPIQYKFAQPRNSNGLKKaSDAAGTPEPTKKgmRLQNLEVRSPPLVLR 191
Cdd:PRK03918 330 IKELEEKEERLeelkkKLKELEKRLEELEERHELYEEAKAKKEELERLKK-RLTGLTPEKLEK--ELEELEKAKEEIEEE 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 192 rcgpnlLEDARAKIRNLSNI----RDNVEMIKV----------------RKQLAEKSSA-LAAMESKFLQLQENQRNFK- 249
Cdd:PRK03918 407 ------ISKITARIGELKKEikelKKAIEELKKakgkcpvcgrelteehRKELLEEYTAeLKRIEKELKEIEEKERKLRk 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 250 --TNHDVLIAKSEELnVQLKEERSKCLHLEKELQSVAIskrrtEELEERvndlEREKELLKENCDKLSSSVFSMTREQEw 327
Cdd:PRK03918 481 elRELEKVLKKESEL-IKLKELAEQLKELEEKLKKYNL-----EELEKK----AEEYEKLKEKLIKLKGEIKSLKKELE- 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 328 klKEEQLKLQIAELETAIQSSLADKDEILGKLKVERDKKEKLMEEN-KDLQSCY---LENKQQLDELKDYMKYLtKRCDV 403
Cdd:PRK03918 550 --KLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERlKELEPFYneyLELKDAEKELEREEKEL-KKLEE 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 404 DVAELSEALLLIKVRKEQKKNgDLICLEK--DDDDIQKVSERsMRKLQLAHA---ETVQELEKTRSMLIVQHKINKGYQT 478
Cdd:PRK03918 627 ELDKAFEELAETEKRLEELRK-ELEELEKkySEEEYEELREE-YLELSRELAglrAELEELEKRREEIKKTLEKLKEELE 704
|
490
....*....|....
gi 2024349576 479 EIEAVTQKMESLQK 492
Cdd:PRK03918 705 EREKAKKELEKLEK 718
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
37-391 |
3.74e-04 |
|
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: 44.81 E-value: 3.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 37 RQAVSQFS-RKELEDkyLQLRDEniSLKQHANKQEETIKRMATRLIQLVHDKKRNEQVGGgpkRLGRTVKMEGMVEHLQE 115
Cdd:pfam10174 127 RQAKELFLlRKTLEE--MELRIE--TQKQTLGARDESIKKLLEMLQSKGLPKKSGEEDWE---RTRRIAEAEMQLGHLEV 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 116 RVRDLEKQNEILRSKLisnkqqihmpsHRPIQYKfAQPRNSNGLKKASDAAGTPEPT-KKGMRLQNLEVRSpplvLRRCG 194
Cdd:pfam10174 200 LLDQKEKENIHLREEL-----------HRRNQLQ-PDPAKTKALQTVIEMKDTKISSlERNIRDLEDEVQM----LKTNG 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 195 PNLLEDARAKIRNLSNIRDNVEMIK-----VRKQLAEKSSALAAMESKFLQLQENQRNFKTNHDVLiakSEELNVqlKEE 269
Cdd:pfam10174 264 LLHTEDREEEIKQMEVYKSHSKFMKnkidqLKQELSKKESELLALQTKLETLTNQNSDCKQHIEVL---KESLTA--KEQ 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 270 RSKCLHLEkelqsVAISKRRTEELEERVNDLEREKELLKENCDKLSSSVFSMTREQEWKLKE------------EQLK-- 335
Cdd:pfam10174 339 RAAILQTE-----VDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKinvlqkkienlqEQLRdk 413
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024349576 336 -LQIAELETAIQS-----------------SLADKDEILGKLKVERDKKEK-LMEENKDLQSCYLENKQQLDELK 391
Cdd:pfam10174 414 dKQLAGLKERVKSlqtdssntdtalttleeALSEKERIIERLKEQREREDReRLEELESLKKENKDLKEKVSALQ 488
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
47-460 |
4.68e-04 |
|
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: 44.63 E-value: 4.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 47 ELEDKYLQLRDENISLKQHANKQEETIKRMATRLIQLVHDKKRN-EQVGGGPKRLGRTVK----MEGMVEHLQERVRDLE 121
Cdd:TIGR04523 222 ELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIkKQLSEKQKELEQNNKkikeLEKQLNQLKSEISDLN 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 122 KQ-----NEILRSKLISNKQQIhmpshRPIQYKFAQprNSNGLKKASDAAGTPEPTKKGMRLQNLEVRspplvlrrcgpN 196
Cdd:TIGR04523 302 NQkeqdwNKELKSELKNQEKKL-----EEIQNQISQ--NNKIISQLNEQISQLKKELTNSESENSEKQ-----------R 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 197 LLEDARAKIRNLsnIRDNVEMIKVRKQLAEKSSALaamESKFLQLQENQRNFKTNhdvliAKSEELNVQLKEERSKCLHL 276
Cdd:TIGR04523 364 ELEEKQNEIEKL--KKENQSYKQEIKNLESQINDL---ESKIQNQEKLNQQKDEQ-----IKKLQQEKELLEKEIERLKE 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 277 EKELQSVAIS--KRRTEELEERVNDLEREKELLKENCDKLSSSVFSMTREQEWKLKE--------EQLKLQIAELETAI- 345
Cdd:TIGR04523 434 TIIKNNSEIKdlTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKElkskekelKKLNEEKKELEEKVk 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 346 -----QSSLADKDEILGKLKVE-----RDKKEKLMEENKDLQSCYLE-----NKQQLDELKDYMKYLTK---RCDVDVAE 407
Cdd:TIGR04523 514 dltkkISSLKEKIEKLESEKKEkeskiSDLEDELNKDDFELKKENLEkeideKNKEIEELKQTQKSLKKkqeEKQELIDQ 593
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2024349576 408 LSEALLliKVRKEQKKNGDLIC-LEKDDDDIQKVSER---SMRKLQLAHAETVQELE 460
Cdd:TIGR04523 594 KEKEKK--DLIKEIEEKEKKISsLEKELEKAKKENEKlssIIKNIKSKKNKLKQEVK 648
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
260-523 |
5.45e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.54 E-value: 5.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 260 EELNVQLKE--------ERSKCLHLEKELQSVAISKRRTEELEERVNDLEREKELLKENCDKLsssvfsMTREQEWKLKE 331
Cdd:COG1196 196 GELERQLEPlerqaekaERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEEL------EAELAELEAEL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 332 EQLKLQIAELETAIQSSLADKDEILGKLKVERDKKEKLMEENKDLQSCYLENKQQLDELKdymkyltKRCDVDVAELSEA 411
Cdd:COG1196 270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELE-------EELEELEEELEEL 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 412 LLLIKVRKEQKKngDLICLEKDDDDIQKVSERSMRKLQLAHAETVQELEKTRSMLIVQHKINKGYQTEIEAVTQKMESLQ 491
Cdd:COG1196 343 EEELEEAEEELE--EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLE 420
|
250 260 270
....*....|....*....|....*....|..
gi 2024349576 492 KDYELKIGKYVDLLDMKAARIKKLEAQLRDVA 523
Cdd:COG1196 421 EELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
233-413 |
5.84e-04 |
|
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: 42.99 E-value: 5.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 233 AMESKFLQLQENQRnfktnHDVLIAKSEELNVQLKEERSKclhLEKELQSVaisKRRTEELEERVNDLEREKELLKENCD 312
Cdd:COG1579 1 AMPEDLRALLDLQE-----LDSELDRLEHRLKELPAELAE---LEDELAAL---EARLEAAKTELEDLEKEIKRLELEIE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 313 KLS----------SSVFSmTREQEWKLKE-EQLKLQIAELETAIQSSLADKDEILGKLKVERDKKEKLMEENKDLQScyl 381
Cdd:COG1579 70 EVEarikkyeeqlGNVRN-NKEYEALQKEiESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKA--- 145
|
170 180 190
....*....|....*....|....*....|..
gi 2024349576 382 ENKQQLDELKDYMKYLTKRCDVDVAELSEALL 413
Cdd:COG1579 146 ELDEELAELEAELEELEAEREELAAKIPPELL 177
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
99-460 |
5.88e-04 |
|
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: 44.29 E-value: 5.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 99 RLGRTVKMEGMVEHLQERVRDLEKQNEILRSKLISNKQQIHmpshrpiQYKfaqprnsnglKKASDAAGTPEPTKKgmRL 178
Cdd:TIGR02169 665 GILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLD-------ELS----------QELSDASRKIGEIEK--EI 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 179 QNLEVRSPPLVLRrcgpnlLEDARAKIRNLSNIRDNV--EMIKVRKQLAEKSSALAAmeskfLQLQENQRNFKTNHDVLI 256
Cdd:TIGR02169 726 EQLEQEEEKLKER------LEELEEDLSSLEQEIENVksELKELEARIEELEEDLHK-----LEEALNDLEARLSHSRIP 794
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 257 AKSEELNvQLKEERSKclhLEKelqsvaiskrRTEELEERVNDLEREKELLKEncdklsssvfsmtreqewklKEEQLKL 336
Cdd:TIGR02169 795 EIQAELS-KLEEEVSR---IEA----------RLREIEQKLNRLTLEKEYLEK--------------------EIQELQE 840
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 337 QIAELETAIQSSLADKDEILGKLKVERDKKEKLMEENKDLQSCYLENKQQLDELKDYMKYLTKRCDVDVAELSEALLLIK 416
Cdd:TIGR02169 841 QRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLS 920
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2024349576 417 VRKEQK--KNGDLICLEKDDDDIQKVSER--SMRKLQlahaETVQELE 460
Cdd:TIGR02169 921 ELKAKLeaLEEELSEIEDPKGEDEEIPEEelSLEDVQ----AELQRVE 964
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
216-372 |
7.66e-04 |
|
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: 42.60 E-value: 7.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 216 EMIKVRKQLAEKSSALAAMESKFLQLQENQRNFKTNHDVLIAKSEELNVQLKEERSKCLHLEKELQSVaiskRRTEELEe 295
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV----RNNKEYE- 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024349576 296 rvnDLEREKELLKENCDKLSSSVFS-MTREQEWKLKEEQLKLQIAELETAIQSSLADKDEILGKLKVERDKKEKLMEE 372
Cdd:COG1579 93 ---ALQKEIESLKRRISDLEDEILElMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREE 167
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
35-528 |
7.79e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.80 E-value: 7.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 35 KARQAVSQFSRKELEDKYLQLRDENISLKQHANKQEETIKRMA-----TRLI--QLVHDKKRNEQVGGGPKRLGRTVKME 107
Cdd:TIGR00618 455 KLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLelqeePCPLcgSCIHPNPARQDIDNPGPLTRRMQRGE 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 108 GMVEHLQERVRDLEKQNEILRSKLISNKQQIHMPSHRpiQYKFAQPRNSngLKKASDaagtpeptkkgmRLQNLEVRSPP 187
Cdd:TIGR00618 535 QTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQS--FSILTQCDNR--SKEDIP------------NLQNITVRLQD 598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 188 LV--LRRCGPNLLEDARAKIRNLSNIRDNVEMIKVRKQLAEKSS-ALAAMESKFLQL-QENQRNFKTNHDVLIAKSEELN 263
Cdd:TIGR00618 599 LTekLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELAlKLTALHALQLTLtQERVREHALSIRVLPKELLASR 678
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 264 -VQLKEERSKCLHLEKELQSVAISKRRTEELEERVNDLERE-----------KELLKENCDKLSSSVFSMTREQEWKLKE 331
Cdd:TIGR00618 679 qLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREfneienassslGSDLAAREDALNQSLKELMHQARTVLKA 758
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 332 EQLKLQIAELETAIQSSLADKdeiLGKLKVERDKKEKLMEEnkDLQSCYLENKQQLDELKDYMKYLTKRCDVDVAELSEa 411
Cdd:TIGR00618 759 RTEAHFNNNEEVTAALQTGAE---LSHLAAEIQFFNRLREE--DTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQ- 832
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 412 lLLIKVRKEQKKNGDLICLEKDDDDIQKVSERSMRKlqlaHAETVQELEKT--RSMLIVQHKINKGYQTEIEAVTQKMES 489
Cdd:TIGR00618 833 -FLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQE----QAKIIQLSDKLngINQIKIQFDGDALIKFLHEITLYANVR 907
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 2024349576 490 LQKDYELKI-GKYvdLLDMKAARIKKLEAQLRDVAYGSKR 528
Cdd:TIGR00618 908 LANQSEGRFhGRY--ADSHVNARKYQGLALLVADAYTGSV 945
|
|
| C2A_Ferlin |
cd08373 |
C2 domain first repeat in Ferlin; Ferlins are involved in vesicle fusion events. Ferlins and ... |
772-874 |
8.13e-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: 8.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 772 HDTRIIPSSSNPQIDDHmcFQVPMTADLDQYlkwESLTFYVFDDSEMGEDGFLGKANVPLIPLACNRSISGTFEVTDSER 851
Cdd:cd08373 28 KKTRVLENELNPVWNET--FEWPLAGSPDPD---ESLEIVVKDYEKVGRNRLIGSATVSLQDLVSEGLLEVTEPLLDSNG 102
|
90 100
....*....|....*....|....
gi 2024349576 852 RVTGA-IRVELKwkfaYLSPSGAA 874
Cdd:cd08373 103 RPTGAtISLEVS----YQPPDGAV 122
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
46-522 |
8.70e-04 |
|
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: 43.47 E-value: 8.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 46 KELEDKYLQLRDENISLKQHANKQEETIKRMATRLIQLVHDKKRNEqvgggpkrlgrtvKMEGMVEHLQERVRDLEKQNE 125
Cdd:TIGR04523 169 EELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNK-------------SLESQISELKKQNNQLKDNIE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 126 ILRSKLISNKQQIHMPSHRPIQYKFAQPRNSNGLKKAsdaagTPEPTKKGMRLQNLEvrspplvlrrcgpNLLEDARAKI 205
Cdd:TIGR04523 236 KKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEK-----QKELEQNNKKIKELE-------------KQLNQLKSEI 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 206 RNLSNIRDNVEMIKVRKQLAEK-------SSALAAMESKFLQLQENQRNFKTNHDVLIAKSEELNVQLKEERSKCLHLEK 278
Cdd:TIGR04523 298 SDLNNQKEQDWNKELKSELKNQekkleeiQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKK 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 279 ELQSvaiSKRRTEELEERVNDLEREKELLKENCDKLSSSVFSMTREQEWKLKEEQ---------------LKLQIAELET 343
Cdd:TIGR04523 378 ENQS---YKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIErlketiiknnseikdLTNQDSVKEL 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 344 AIQSSLADKDEILGKLKVERDKKEKLMEENKDLQSCYLENKQQLDELKDYMKYLTKRCDVDVAELSEALLLIKVRKEQKK 423
Cdd:TIGR04523 455 IIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKK 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 424 NGDLICLEKDDDDIQKVSERSMRKLQlahaETVQELEKTrsmlIVQHKINkgyQTEIEAVTQKMESLQKDYELKIGKYVD 503
Cdd:TIGR04523 535 EKESKISDLEDELNKDDFELKKENLE----KEIDEKNKE----IEELKQT---QKSLKKKQEEKQELIDQKEKEKKDLIK 603
|
490
....*....|....*....
gi 2024349576 504 LLDMKAARIKKLEAQLRDV 522
Cdd:TIGR04523 604 EIEEKEKKISSLEKELEKA 622
|
|
| C2_C21orf25-like |
cd08678 |
C2 domain found in the Human chromosome 21 open reading frame 25 (C21orf25) protein; The ... |
772-871 |
9.20e-04 |
|
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: 9.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 772 HDTRIIPSSSNPQIDDHMCFQV-PMTADLdqylkweslTFYVFDDSEMGEDGFLGKANVPLIPLACNRSISGTFE---VT 847
Cdd:cd08678 33 YQSSTQKNTSNPFWDEHFLFELsPNSKEL---------LFEVYDNGKKSDSKFLGLAIVPFDELRKNPSGRQIFPlqgRP 103
|
90 100
....*....|....*....|....
gi 2024349576 848 DSERRVTGAIRVElkwkFAYLSPS 871
Cdd:cd08678 104 YEGDSVSGSITVE----FLFMEPA 123
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
188-519 |
9.94e-04 |
|
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: 43.27 E-value: 9.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 188 LVLRRCGPNLLEDARAKIRNLSNIRDNVemikvrKQLAEKSS----ALAAMESKflqLQENQR---NFKTNHD----VLI 256
Cdd:pfam10174 397 NVLQKKIENLQEQLRDKDKQLAGLKERV------KSLQTDSSntdtALTTLEEA---LSEKERiieRLKEQREredrERL 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 257 AKSEELNVQLKEERSKCLHLEKELQsvaiskrrteELEERVNDLEREKELLKENCDKLSSSVFSMTREQEWKlKEEQLKL 336
Cdd:pfam10174 468 EELESLKKENKDLKEKVSALQPELT----------EKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQK-KEECSKL 536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 337 QiAELETAIQSSLAD--KDEILGKLKV-ERDKKEKLMEENKdlqsCYLENKQQLDELKDY-MKYLTKrcDVDVAELsEAL 412
Cdd:pfam10174 537 E-NQLKKAHNAEEAVrtNPEINDRIRLlEQEVARYKEESGK----AQAEVERLLGILREVeNEKNDK--DKKIAEL-ESL 608
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 413 LLIKVRKEQKKNGDLICLEKDD--------DDIQKVSERSMRK-LQLAHAETVQELEKTRSmlivqhkinkgyqtEIEAV 483
Cdd:pfam10174 609 TLRQMKEQNKKVANIKHGQQEMkkkgaqllEEARRREDNLADNsQQLQLEELMGALEKTRQ--------------ELDAT 674
|
330 340 350
....*....|....*....|....*....|....*.
gi 2024349576 484 TQKMESLQKDYELKIGKyvdLLDMKAARIKKLEAQL 519
Cdd:pfam10174 675 KARLSSTQQSLAEKDGH---LTNLRAERRKQLEEIL 707
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
198-529 |
1.37e-03 |
|
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: 43.17 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 198 LEDARAKIRNLSNIRDNVEMIKVRKQ-------LAEKSSALAAMESKFLQLQENQR----NFKTNHDVLIAKSEELNVQ- 265
Cdd:pfam05483 127 FENEKVSLKLEEEIQENKDLIKENNAtrhlcnlLKETCARSAEKTKKYEYEREETRqvymDLNNNIEKMILAFEELRVQa 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 266 ----------LKEERSKCLHLEKELQSVAISKRRTEEL-----EERVNDLEREKELLKENCDKLSSsvfsmtREQEWKLK 330
Cdd:pfam05483 207 enarlemhfkLKEDHEKIQHLEEEYKKEINDKEKQVSLlliqiTEKENKMKDLTFLLEESRDKANQ------LEEKTKLQ 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 331 EEQLKlQIAELETAIQSSLAD-KDEILGKLKVERDKKEKLMEENKDLQSCYLENKQQLDEL---KDYMKYLTKRCDVDVA 406
Cdd:pfam05483 281 DENLK-ELIEKKDHLTKELEDiKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELnkaKAAHSFVVTEFEATTC 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 407 ELSEALllikvRKEQKKngdlicLEKDDDDIQKVSERSMRKlqLAHAETVQELEKTRSMLIVQHKINKGYQTEIEAVTQK 486
Cdd:pfam05483 360 SLEELL-----RTEQQR------LEKNEDQLKIITMELQKK--SSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQ 426
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2024349576 487 MESLQKDYELKIGKYVDLLDMKAARIKKLEAQLRDVAYGSKRY 529
Cdd:pfam05483 427 FEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHY 469
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
198-521 |
1.37e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 198 LEDARAKIRNLSNIRDNVEmikvrKQLAEKSSALAAMESKFLQLQENQRNFKTNHDVLIAKSEELNVQLKEERS------ 271
Cdd:PRK02224 372 LEEAREAVEDRREEIEELE-----EEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARErveeae 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 272 ------KCLHLEKELQ------SVAISKRRTEELEERVNDLEREKELLKENCDKLSSSVFSMTREQEWKLKEEQLKLQIA 339
Cdd:PRK02224 447 alleagKCPECGQPVEgsphveTIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIA 526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 340 ELET-------AIQSSLADKDEILGKLKVERDKKEKLMEENKDLQSCYLENKQQLDELKDYMKYLTKRCDVdVAELSEAL 412
Cdd:PRK02224 527 ERREtieekreRAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTL-LAAIADAE 605
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 413 LLIKVRKEQKKNGDliclEKDDDDIQKVSERSMRKLQLAHAETVQELEKTRSmlivQHKINKGYQTEIEAVTQKMESLQK 492
Cdd:PRK02224 606 DEIERLREKREALA----ELNDERRERLAEKRERKRELEAEFDEARIEEARE----DKERAEEYLEQVEEKLDELREERD 677
|
330 340
....*....|....*....|....*....
gi 2024349576 493 DYELKIGkyvdlldMKAARIKKLEAqLRD 521
Cdd:PRK02224 678 DLQAEIG-------AVENELEELEE-LRE 698
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
23-390 |
1.75e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 42.74 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 23 RVRGLLASARNVKARQAVSQFSRKELEDKYLQLRDENISLKQHANKQEETIKRMATRLIQLvhdkkrneqvgggpkrlgr 102
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL------------------- 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 103 tvkmEGMVEHLQERVRDLEKQNEILRSKLISNKQQIHmPSHRPIQYKFAQPRNSNGLKKASDAAGtpepTKKGMRLQNLE 182
Cdd:TIGR02168 746 ----EERIAQLSKELTELEAEIEELEERLEEAEEELA-EAEAEIEELEAQIEQLKEELKALREAL----DELRAELTLLN 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 183 VRSPPLVLRRcgPNLLEDARAKIRNLSNIrdnvemikvRKQLAEKSSALAAMESKFLQLQENQRNFKTNHDVLIAKSEEL 262
Cdd:TIGR02168 817 EEAANLRERL--ESLERRIAATERRLEDL---------EEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASL 885
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 263 NVQLKEERSKCLHLEKELQsvaiskrrteELEERVNDLEREKELLKEncdKLSSSvfsmtreqewKLKEEQLKLQIAELE 342
Cdd:TIGR02168 886 EEALALLRSELEELSEELR----------ELESKRSELRRELEELRE---KLAQL----------ELRLEGLEVRIDNLQ 942
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2024349576 343 TAIQSSLADKDEILGKLKVERDKK-EKLMEENKDLqscylenKQQLDEL 390
Cdd:TIGR02168 943 ERLSEEYSLTLEEAEALENKIEDDeEEARRRLKRL-------ENKIKEL 984
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
332-521 |
1.85e-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: 42.06 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 332 EQLKLQIAELETAIQSSLADKDEILGKLKVERDKKEKLMEENKDLQSCYLENKQQLDELKDYMKYLTKRCDVDVAELSEa 411
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 412 lLLIKVRKEQKKNGDLICLEKDDDDIQKVSERSMRKLQLAHAETVQELEKTRSMLIVQHKINKGYQTEIEAVTQKMESLQ 491
Cdd:COG4942 109 -LLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEER 187
|
170 180 190
....*....|....*....|....*....|
gi 2024349576 492 KDYELKIGKYVDLLDMKAARIKKLEAQLRD 521
Cdd:COG4942 188 AALEALKAERQKLLARLEKELAELAAELAE 217
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
216-521 |
1.92e-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: 42.47 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 216 EMIKVRKQLAEKSSALAAMESKFLQLQEN----QRNFKTNHDvLIAKSEELNVQL---KEERSKCLHlekELQSvaiskr 288
Cdd:pfam01576 13 ELQKVKERQQKAESELKELEKKHQQLCEEknalQEQLQAETE-LCAEAEEMRARLaarKQELEEILH---ELES------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 289 RTEELEERVNDLEREKELLKENCDKLsssvfsmtreqEWKLKEEQLKLQIAELETAIQSSLADK--DEILgklkVERDKK 366
Cdd:pfam01576 83 RLEEEEERSQQLQNEKKKMQQHIQDL-----------EEQLDEEEAARQKLQLEKVTTEAKIKKleEDIL----LLEDQN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 367 EKLMEENKDLQSCYLENKQQLDELKDYMKYLTKRCDVDVAELSEalLLIKVRKEQKKNGDLiclekddDDIQKVSERSMR 446
Cdd:pfam01576 148 SKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISD--LEERLKKEEKGRQEL-------EKAKRKLEGEST 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024349576 447 KLQLAHAETVQELEKTRSMLIVQHKINKGYQTEIE-AVTQKMESLQKDYELKIGK---YVDLLDMKAARiKKLEAQLRD 521
Cdd:pfam01576 219 DLQEQIAELQAQIAELRAQLAKKEEELQAALARLEeETAQKNNALKKIRELEAQIselQEDLESERAAR-NKAEKQRRD 296
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
219-518 |
2.01e-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: 42.65 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 219 KVRKQLAEKSSALAAMESKFLQLQENQRNFKTNHDVLIAKSEELNvQLKEERSKCLHLEKELQSVAISKRRTEELEERV- 297
Cdd:TIGR00618 163 KEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLT-LCTPCMPDTYHERKQVLEKELKHLREALQQTQQs 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 298 -NDLEREKELLKENCDKLSSSVFSMTREQEWKLKEEQLKLQ------------IAELETAIQSSLADKDEILGKLKVERD 364
Cdd:TIGR00618 242 hAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETqerinrarkaapLAAHIKAVTQIEQQAQRIHTELQSKMR 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 365 KKEKLMEENKDL--QSCYLENKQQL--------DELKDYMKYLTKRCDVDVAELSE-----ALLLIKVRKEQKKNGDLIC 429
Cdd:TIGR00618 322 SRAKLLMKRAAHvkQQSSIEEQRRLlqtlhsqeIHIRDAHEVATSIREISCQQHTLtqhihTLQQQKTTLTQKLQSLCKE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 430 LEKDDDDIQKV----SERSMRKLQLAHAETVQELEKTRSMLIVQHkINKGYQTEIEAVTQKMESLQKDYELKIG-KYVDL 504
Cdd:TIGR00618 402 LDILQREQATIdtrtSAFRDLQGQLAHAKKQQELQQRYAELCAAA-ITCTAQCEKLEKIHLQESAQSLKEREQQlQTKEQ 480
|
330
....*....|....
gi 2024349576 505 LDMKAARIKKLEAQ 518
Cdd:TIGR00618 481 IHLQETRKKAVVLA 494
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
241-406 |
2.50e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.00 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 241 LQENQRNFKTNHDVLIAKSEELNVQLKEERSKCLHLEKELQSVAISK--RRTEELEERVNDLEREKELLKENCDKLSssv 318
Cdd:PRK12705 39 LQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERlvQKEEQLDARAEKLDNLENQLEEREKALS--- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 319 fsmTREQEWKLKEEQLKLQIaeLETAIQSSLADKDEILGKLKVERdKKEKLMEENKDLQSCYLENKQqldELKDYMKYLT 398
Cdd:PRK12705 116 ---ARELELEELEKQLDNEL--YRVAGLTPEQARKLLLKLLDAEL-EEEKAQRVKKIEEEADLEAER---KAQNILAQAM 186
|
....*...
gi 2024349576 399 KRCDVDVA 406
Cdd:PRK12705 187 QRIASETA 194
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
34-384 |
2.68e-03 |
|
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: 42.02 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 34 VKARQAVSQFSRKELEDKYLQLRDE---NISLKQHANKQEETIKRMATRLIQLVHD-KKRNEQVGGGPKRLGRTVKMegm 109
Cdd:pfam05483 459 LTAIKTSEEHYLKEVEDLKTELEKEklkNIELTAHCDKLLLENKELTQEASDMTLElKKHQEDIINCKKQEERMLKQ--- 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 110 VEHLQERVRDLEKQNEILRSKLISNKQQIHMP------SHRPIQYKFAQPRNSNGLKKASDAAGTPEPTKKGMRLQNLEV 183
Cdd:pfam05483 536 IENLEEKEMNLRDELESVREEFIQKGDEVKCKldkseeNARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQ 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 184 RSPPLvlrrcgpnlledarAKIRNLSNIRDNVEMIKVRKQLAEKSSALAAMESKFLQLQENQRNFKTNHDVLIAKSEELN 263
Cdd:pfam05483 616 ENKAL--------------KKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAK 681
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 264 VQLKEerskCLHLEKElqsvaISKRRTEELEERVNDLEREKELLKENCDKLSSSV-FSMTREQEWKLKEEQLKLQIAELE 342
Cdd:pfam05483 682 AIADE----AVKLQKE-----IDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELgLYKNKEQEQSSAKAALEIELSNIK 752
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2024349576 343 TAIQSsladkdeILGKLKVERDKKEKLMEENKDLQSCYLENK 384
Cdd:pfam05483 753 AELLS-------LKKQLEIEKEEKEKLKMEAKENTAILKDKK 787
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
218-520 |
2.72e-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: 41.93 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 218 IKVRKQLAEKSSALAAMESKFLQLQENQRNFKTNHDVLIAKSEELNVQLKEERSKCLHLEKELQSVAISKRRTEELEERV 297
Cdd:TIGR04523 141 DKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQI 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 298 NDLEREKELLKENCDKLSS------SVFSMTREQEWKLKEE------QLKLQIAELETAiQSSLADKDEILGKLKVERD- 364
Cdd:TIGR04523 221 SELKKQNNQLKDNIEKKQQeinektTEISNTQTQLNQLKDEqnkikkQLSEKQKELEQN-NKKIKELEKQLNQLKSEISd 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 365 -KKEKLMEENKDLQSCYLENKQQLDELKDymkyltkrcdvdvaELSEALLLIKVRKEQKKNgdlicLEKDDDDiqKVSER 443
Cdd:TIGR04523 300 lNNQKEQDWNKELKSELKNQEKKLEEIQN--------------QISQNNKIISQLNEQISQ-----LKKELTN--SESEN 358
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024349576 444 SMRKLQLahAETVQELEKTRsmlivqhKINKGYQTEIeavtQKMESLQKDYELKIGKYVDLLDMKAARIKKLEAQLR 520
Cdd:TIGR04523 359 SEKQREL--EEKQNEIEKLK-------KENQSYKQEI----KNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKE 422
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
198-374 |
2.76e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 198 LEDARAKIRNLSNIRDNVEmiKVRKQLAEKSSALAAMESKFLQLQENQRNFKTNHDV--LIAKSEELNVQLKEERSKCLH 275
Cdd:COG4717 73 LKELEEELKEAEEKEEEYA--ELQEELEELEEELEELEAELEELREELEKLEKLLQLlpLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 276 LEKELQSVAISKRRTEELEERVNDLEREKELLKENCDKLSSSvfsmtREQEWKLKEEQLKLQIAELETAIQSSLADKDEI 355
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEE-----ELQDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
170
....*....|....*....
gi 2024349576 356 LGKLKVERDKKEKLMEENK 374
Cdd:COG4717 226 EEELEQLENELEAAALEER 244
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
198-449 |
3.05e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.05 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 198 LEDARAKIRNLSNIRDnvemiKVRKQLAEKSSALAAMESKFLQLQENQRNFKTNHDVLIAKSEELNVQLKEERSKCLHLE 277
Cdd:COG1340 31 RDELNEELKELAEKRD-----ELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 278 KELQSVAISKRRTEELEER----VNDLEREKEL------LKENCDKLSSSvfsmtREQEWKLKE-----EQLKLQIAELE 342
Cdd:COG1340 106 KAGGSIDKLRKEIERLEWRqqteVLSPEEEKELvekikeLEKELEKAKKA-----LEKNEKLKElraelKELRKEAEEIH 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 343 TAIQSSLADKDEILGKLKVERDKKEKLMEENKDLQSCYLENKQQLDELKdymkyltKRCDVDVAELSEallLIKVRKEQK 422
Cdd:COG1340 181 KKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELH-------EEIIELQKELRE---LRKELKKLR 250
|
250 260
....*....|....*....|....*..
gi 2024349576 423 KNGDLICLEKDDDDIQKVSERSMRKLQ 449
Cdd:COG1340 251 KKQRALKREKEKEELEEKAEEIFEKLK 277
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
291-407 |
3.59e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.61 E-value: 3.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 291 EELEERVNDLEREKELLKENCDKLSSSvfsmtREQEWKLKEEQLKLQIAELETAIQSSLADKDEIlgklkveRDKKEKLM 370
Cdd:COG0542 414 DELERRLEQLEIEKEALKKEQDEASFE-----RLAELRDELAELEEELEALKARWEAEKELIEEI-------QELKEELE 481
|
90 100 110
....*....|....*....|....*....|....*...
gi 2024349576 371 EENKDLQSCYLENKQQLDELKDYMKYLTKRCDV-DVAE 407
Cdd:COG0542 482 QRYGKIPELEKELAELEEELAELAPLLREEVTEeDIAE 519
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
260-522 |
3.82e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.56 E-value: 3.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 260 EELNVQLKEERSKCLH-----LEKELQSVaiskrrTEELEErvndLEREKELLKENCDKLSSsvfsMTREQEWKLKE-EQ 333
Cdd:PRK02224 190 DQLKAQIEEKEEKDLHerlngLESELAEL------DEEIER----YEEQREQARETRDEADE----VLEEHEERREElET 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 334 LKLQIAELETAIQSSLADKDEILGKLKVERDKKEKLMEENKD-LQSCYLEN------KQQLDELKDymkyltkrcdvDVA 406
Cdd:PRK02224 256 LEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDlLAEAGLDDadaeavEARREELED-----------RDE 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 407 ELSEALLLIKVRKEQKKNGdlicLEKDDDDIQKVSERSMRKLQLAhAETVQELEKTRSmlivqhKINKGyQTEIEAVTQK 486
Cdd:PRK02224 325 ELRDRLEECRVAAQAHNEE----AESLREDADDLEERAEELREEA-AELESELEEARE------AVEDR-REEIEELEEE 392
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2024349576 487 MESLQK---DYELKIGKYVDLLDMKAA-------RIKKLEAQLRDV 522
Cdd:PRK02224 393 IEELRErfgDAPVDLGNAEDFLEELREerdelreREAELEATLRTA 438
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
227-468 |
3.99e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 227 KSSALAAMESKFL-QLQENQRN-FKT---NHDVLIAKSEELNVQLKEERSKCLHLEKELQSVAISKRRTEELEERVNDLE 301
Cdd:COG4717 36 KSTLLAFIRAMLLeRLEKEADElFKPqgrKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 302 REKELLKEncdklsssvfsMTREQEWKLKEEQLKLQIAELETAIQSSLADKDEILGKLKVERDKKEKLMEENKDLQSCY- 380
Cdd:COG4717 116 EELEKLEK-----------LLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLe 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 381 ---LENKQQLDELKDYMKYLTKRcdvdVAELSEALLLIKVRKEQkkngdlicLEKDDDDIQKvsersmrklQLAHAETVQ 457
Cdd:COG4717 185 qlsLATEEELQDLAEELEELQQR----LAELEEELEEAQEELEE--------LEEELEQLEN---------ELEAAALEE 243
|
250
....*....|.
gi 2024349576 458 ELEKTRSMLIV 468
Cdd:COG4717 244 RLKEARLLLLI 254
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
51-393 |
4.25e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 41.10 E-value: 4.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 51 KYLQLRDENISLKQHANKQEETIKRMATRLIQLVH--DKKRNEQVGGGPKRLGR----TVKMEGMVEHLQERVRDLEKQN 124
Cdd:COG5185 226 KEIINIEEALKGFQDPESELEDLAQTSDKLEKLVEqnTDLRLEKLGENAESSKRlnenANNLIKQFENTKEKIAEYTKSI 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 125 EILRSKLISNKQqihmpshrpiqykFAQPRnsnglKKASDAAGTPEPTKKGMRLQNlevrspplVLRRCGPNLLEDARAK 204
Cdd:COG5185 306 DIKKATESLEEQ-------------LAAAE-----AEQELEESKRETETGIQNLTA--------EIEQGQESLTENLEAI 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 205 IRNLSNIRDNVEMIKVRKQLAEKSSALAAMESKFLQLQENQRNFKtnHDVLIAKSEELNVQLKEERSKCLHLEKELQSVA 284
Cdd:COG5185 360 KEEIENIVGEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYA--QEILATLEDTLKAADRQIEELQRQIEQATSSNE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 285 ISKRRTEELEERVNDLERE-----KELLKENCDKLSSSVFSMTREQEwkLKEEQLKLQIAELETAIQSSLADKDEILGKL 359
Cdd:COG5185 438 EVSKLLNELISELNKVMREadeesQSRLEEAYDEINRSVRSKKEDLN--EELTQIESRVSTLKATLEKLRAKLERQLEGV 515
|
330 340 350
....*....|....*....|....*....|....*...
gi 2024349576 360 KVERDKKEK----LMEENKDLQSCYLENKQQLDELKDY 393
Cdd:COG5185 516 RSKLDQVAEslkdFMRARGYAHILALENLIPASELIQA 553
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
220-375 |
5.39e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 5.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 220 VRKQLAEKSSALAAMESKFLqLQENQRNFKTNHD--VLIAKSEELNVQ------LKEERSKCLHLEKELQsvaiskRRTE 291
Cdd:PRK12704 24 VRKKIAEAKIKEAEEEAKRI-LEEAKKEAEAIKKeaLLEAKEEIHKLRnefekeLRERRNELQKLEKRLL------QKEE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 292 ELEERVNDLEREKELLKEncdklsssvfsmtREQEWKLKEEQLKLQIAELETAIQSSLADKDEILGkLKVErDKKEKLME 371
Cdd:PRK12704 97 NLDRKLELLEKREEELEK-------------KEKELEQKQQELEKKEEELEELIEEQLQELERISG-LTAE-EAKEILLE 161
|
....
gi 2024349576 372 ENKD 375
Cdd:PRK12704 162 KVEE 165
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
45-319 |
6.78e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.82 E-value: 6.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 45 RKELEDKYLQLRDENI-SLKQHANKQEETIKRMATRLIQLvhDKKRNeqvgggpKRLGRTVKMEGMVEHLQERVRDLEKQ 123
Cdd:TIGR02169 778 EEALNDLEARLSHSRIpEIQAELSKLEEEVSRIEARLREI--EQKLN-------RLTLEKEYLEKEIQELQEQRIDLKEQ 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 124 NEilrskliSNKQQIHmpshrpiqykfaqprNSNGLKKASDAagtpEPTKKGMRLQNLEVRSPPLVLRRcgpnllEDARA 203
Cdd:TIGR02169 849 IK-------SIEKEIE---------------NLNGKKEELEE----ELEELEAALRDLESRLGDLKKER------DELEA 896
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 204 KIRNLSNIRD--NVEMIKVRKQLAEKSSALAAMESKFLQLQENQRNfktnhDVLIAKSEELNVQLKEERSKCLHLEKELQ 281
Cdd:TIGR02169 897 QLRELERKIEelEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGE-----DEEIPEEELSLEDVQAELQRVEEEIRALE 971
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2024349576 282 SV--------AISKRRTEELEERVNDLEREKELLK---ENCDKLSSSVF 319
Cdd:TIGR02169 972 PVnmlaiqeyEEVLKRLDELKEKRAKLEEERKAILeriEEYEKKKREVF 1020
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
149-564 |
7.46e-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: 40.73 E-value: 7.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 149 KFAQPRNSNGLKKASDAAGTPEPTKKGMRLQNLEVRSPPLVLRRCGPNLLEDARAKIRNLSNIRDNVEMIKVRKQLAEKS 228
Cdd:pfam02463 579 KLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGL 658
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 229 salaAMESKFLQLQENQRNFKTNHDVLIAKSEELNVQLKEERSKCLHLEKELQSVAISKRRTEELEERVNDLEREKELLK 308
Cdd:pfam02463 659 ----AEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKI 734
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 309 ENCDKLSSSVFSMTREQEWKLKEEQLKLQIAELE-TAIQSSLADKDEILGKLKVERDKKEKL--MEEnkDLQSCYLENKQ 385
Cdd:pfam02463 735 NEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSElSLKEKELAEEREKTEKLKVEEEKEEKLkaQEE--ELRALEEELKE 812
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 386 QLDELKdymkyltkrcdvDVAELSEALLLIKVRKEQKKNGDLICLEKDDDDIQKVSERSMrKLQLAHAETVQELEKTRSM 465
Cdd:pfam02463 813 EAELLE------------EEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLE-EEITKEELLQELLLKEEEL 879
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024349576 466 LIVQHKINKG--YQTEIEAVTQKMESLQKDYELKIGKYVDLLDMKaaRIKKLEAQLRDVaygSKRYKFRPEILPANPVNI 543
Cdd:pfam02463 880 EEQKLKDELEskEEKEKEEKKELEEESQKLNLLEEKENEIEERIK--EEAEILLKYEEE---PEELLLEEADEKEKEENN 954
|
410 420
....*....|....*....|.
gi 2024349576 544 FDETLHFERREGLFEIHISKV 564
Cdd:pfam02463 955 KEEEEERNKRLLLAKEELGKV 975
|
|
| |
